Ver o código fonte de "Receptor de glicocorticoides"

{{Non confundir|receptor de glicocorticoides de membrana}}
{{Xene-proteína
|nome           = NR3C1
|nomes          = 	NR3C1, GCCR, GCR, GCRST, GR, GRL, receptor nuclear subfamilia 3 grupo C membro 1, receptor de glicocorticoides
|imaxe           = Glucocorticoid receptor.png
|imaxe_tamaño    = 
|imaxe_pé       = 
|HGNCid           =7978
|MGIid            = 95824
|símbolo          = NR3C1
|símbolos_alt     = NR3C1, GCCR, GCR, GCRST, GR, GRL
<!-- Datos xenéticos -->
|Xene              = NR3C1
|Xene_tipo         = codificante de proteínas
|Cromosoma        = 5
|Brazo            = q
|Banda            = 31.3
|LocusSupplementaryData = 
<!-- Estrutura/función proteica -->
|Longo_proteína   = 
|Peso_molecular   = 
|Estrutura       = 
|Tipo             = 
|Funcións        = 
|Dominio          = 
|Motivo           = 
|Produtos_alt    = 
|Función         =
|Compoñente        =
|Proceso          =
<!-- Info adicional -->
|Taxon            = 
|Célula           = 
|Localización        = 
|Modificación     = 
|Ruta             = 
|Interaccións    = 
|Prop_biofisicas  = 
<!-- Datos encimáticos -->
|Act_catalítica   = 
|Cofactores       = 
|Reg_encimática   = 
|Km               = 
|Vmax             = 
<!-- Datos do receptor/ligando -->
|Acción           = 
|Agonista         = 
|Antagonista      = 
<!-- Datos biotecnolóxicos/médicos -->
|Enfermidade       = 
|Fármaco          = 
|Biotecnoloxía    = 
<!-- Bases de datos -->
|Accesión         = 
|ECnumber         = 
|ATC_prefix       = 
|ATC_suffix       = 
|ATC_supplemental = 
|CAS_number       = 
|CAS_supplemental = 
|DrugBank         =
|Homologene       = 30960
|IUPHAR           =
|OMIM             = 138040
|GeneAtlas_image1 =PBB GE NR3C1 216321 s at fs.png
|GeneAtlas_image2 =PBB GE NR3C1 201865 x at fs.png
|GeneAtlas_image3 =PBB GE NR3C1 201866 s at fs.png
|PDB              = {{PDB2|1M2Z}} , {{PDB2|1NHZ}} , {{PDB2|1P93}} , {{PDB2|3BQD}} , {{PDB2|3CLD}} , {{PDB2|3E7C}} , {{PDB2|3H52}} , {{PDB2|3K22}} , {{PDB2|3K23}} , {{PDB2|4CSJ}} , {{PDB2|4HN5}} , {{PDB2|4HN6}} , {{PDB2|4LSJ}} , {{PDB2|4MDD}} , {{PDB2|4P6W}} , {{PDB2|4P6X}} , {{PDB2|5CBY}} , {{PDB2|5CBX}} , {{PDB2|4UDC}} , {{PDB2|4UDD}} , {{PDB2|5CBZ}} , {{PDB2|5CC1}} , {{PDB2|5EMQ}} , {{PDB2|5EMC}} , {{PDB2|5EMP}}
|Varios_PDB       =
|NCBI             =
|KEGG             =
|Orthologs =
<!-- Ortoloxía -->
|Hs_EntrezGene =2908
|Hs_Ensembl =ENSG00000113580
|Hs_RefseqmRNA =NM_000176
|Hs_RefseqProtein =NP_000167
|Hs_GenLoc_db =hg5
|Hs_GenLoc_chr = 5
|Hs_GenLoc_start =143277931
|Hs_GenLoc_end =143435512
|Hs_Uniprot =P04150
|Mm_EntrezGene = 14815
|Mm_Ensembl = ENSMUSG00000024431
|Mm_RefseqmRNA = NM_008173
|Mm_RefseqProtein = NP_001348138
|Mm_GenLoc_db = mm9
|Mm_GenLoc_chr = 18
|Mm_GenLoc_start = 39543598
|Mm_GenLoc_end = 39652474
|Mm_Uniprot = P06537
<!-- Info relacionada -->
|Artigo         = 
|Publicación      = 
}}O '''receptor de glicocorticoides''' ('''GCR''' ou '''GR'''), tamén chamado '''NR3C1''' ([[receptor nuclear]] subfamilia 3, grupo C, membro 1), é o [[Receptor (bioquímica)|receptor]] [[citosol|citosólico]] ao cal se unen o [[cortisol]] e outros [[glicocorticoide]]s.

O GCR [[expresión xénica|exprésase]] en case todas as células do corpo e regula [[xene]]s que controlan o [[bioloxía do desenvolvemento|desenvolvemento]], [[metabolismo]] e [[sistema inmunitario|resposta inmune]]. Como o xene do receptor exprésase de varias formas, ten moitos efectos diferentes ([[pleiotrópico]]s) en diferentes partes do corpo.

Cando os [[glicocorticoide]]s se unen a este receptor, o seu mecanimso primario de acción é a regulación da [[transcrición xénica]].<ref name="Lu">{{cite journal | vauthors = Lu NZ, Wardell SE, Burnstein KL, Defranco D, Fuller PJ, Giguere V, Hochberg RB, McKay L, Renoir JM, Weigel NL, Wilson EM, McDonnell DP, Cidlowski JA | display-authors = 6 | title = International Union of Pharmacology. LXV. The pharmacology and classification of the nuclear receptor superfamily: glucocorticoid, mineralocorticoid, progesterone, and androgen receptors | journal = Pharmacological Reviews | volume = 58 | issue = 4 | pages = 782–797 | date = decembro de 2006 | pmid = 17132855 | doi = 10.1124/pr.58.4.9 }} [texto completo libre]</ref><ref name="pmid16236742">{{cite journal | vauthors = Rhen T, Cidlowski JA | title = Antiinflammatory action of glucocorticoids--new mechanisms for old drugs | journal = The New England Journal of Medicine | volume = 353 | issue = 16 | pages = 1711–1723 | date = outubro de 2005 | pmid = 16236742 | doi = 10.1056/NEJMra050541  }}</ref> O receptor non unido a ligando encóntrase no [[citosol]] da célula. Despois de que o receptor se une a un glicocorticoide, o complexo receptor-glicocorticoide pode tomar dous camiños posibles: o complexo do receptor activado regula á alza a expresión de proteínas antiinflamatorias no [[núcleo celular|núcleo]] ou ben reprime a expresión de proteínas proinflamatorias no citosol (ao impedir a translocación doutros [[factor de transcrición|factores de transcrición]] do citosol ao núcleo).

En humanos, a proteína do receptor de glicocorticoides está codificada polo [[xene]] {{gene|NR3C1}} que está localizado no [[cromosoma 5]] (5q31).<ref name="pmid2867473">{{cite journal | vauthors = Hollenberg SM, Weinberger C, Ong ES, Cerelli G, Oro A, Lebo R, Thompson EB, Rosenfeld MG, Evans RM | display-authors = 6 | title = Primary structure and expression of a functional human glucocorticoid receptor cDNA | journal = Nature | volume = 318 | issue = 6047 | pages = 635–641 | date = decembro de 1985 | pmid = 2867473 | pmc = 6165583 | doi = 10.1038/318635a0 | bibcode = 1985Natur.318..635H }}</ref><ref name="pmid2744768">{{cite journal | vauthors = Francke U, Foellmer BE | title = The glucocorticoid receptor gene is in 5q31-q32 [corrected] | journal = Genomics | volume = 4 | issue = 4 | pages = 610–612 | date = maio de 1989 | pmid = 2744768 | doi = 10.1016/0888-7543(89)90287-5 }}</ref>

Este receptor citosólico actúa por medio de mecanismos xenómicos, e non debe confundirse cos [[receptor de glicocortocoides de membrana|receptores de glicocorticoides de membrana]], que se encontran na superficie celular e actúan por medio de [[cadoiro]]s de sinalización.

== Estrutura ==
Como outros [[receptor de esteroides|receptores de esteroides]],<ref name="pmid10406480">{{cite journal | vauthors = Kumar R, Thompson EB | title = The structure of the nuclear hormone receptors | url = https://archive.org/details/sim_steroids_1999-05_64_5/page/310 | journal = Steroids | volume = 64 | issue = 5 | pages = 310–319 | date = maio de 1999 | pmid = 10406480 | doi = 10.1016/S0039-128X(99)00014-8  }}</ref> o receptor de glicocortocoides ten estrutura modular.<ref name="pmid15876404">{{cite journal | vauthors = Kumar R, Thompson EB | title = Gene regulation by the glucocorticoid receptor: structure:function relationship | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 94 | issue = 5 | pages = 383–394 | date = abril de 2005 | pmid = 15876404 | doi = 10.1016/j.jsbmb.2004.12.046  }}</ref> e contén os seguintes [[dominio proteico|dominios]] (designados do '''A''' ao '''F'''):
* '''A/B''' - dominio regulatorio [[N-terminal]]
* '''C''' - [[dominio de unión ao ADN]] (DBD)
* '''D''' - rexión bisagra
* '''E''' - dominio de unión ao ligando (LBD)
* '''F''' - dominio [[C-terminal]].

== Unión de ligandos e resposta ==
En ausencia de [[hormona]], o receptor de glicocorticoides (GCR) encóntrase no [[citosol]] formando un [[complexo proteico|complexo]] con diversas proteínas, como a [[proteína de choque térmico]] 90 ([[hsp90]]), a proteína de choque térmico 70 ([[hsp70]]) e a proteína [[FKBP4]] (proteína que se une a [[FK506]] 4).<ref name="Pratt">{{cite book | vauthors = Pratt WB, Morishima Y, Murphy M, Harrell M | title = Molecular Chaperones in Health and Disease | chapter = Chaperoning of glucocorticoid receptors | volume = 172 | issue = | pages = 111–138 | year = 2006 | pmid = 16610357 | doi = 10.1007/3-540-29717-0_5 | isbn = 978-3-540-25875-9 | series = Handbook of Experimental Pharmacology }}</ref> A hormona glicocorticoide endóxena [[cortisol]] difunde a través da [[membrana plasmática]] ata o [[citoplasma]] e únese ao receptor de glicocorticoides, causando a liberación das proteínas de choque térmico que formaban o complexo. Como resultado o receptor queda activado e exhibe dous mecanismos principais de acción: transactivación e transrepresión,<ref name="Buckingham">{{cite journal | vauthors = Buckingham JC | title = Glucocorticoids: exemplars of multi-tasking | journal = British Journal of Pharmacology | volume = 147 | issue = Supplement 1 | pages = S258–S268 | date = xaneiro de 2006 | pmid = 16402112 | pmc = 1760726 | doi = 10.1038/sj.bjp.0706456 }}</ref><ref name="Hayashi">{{cite journal | vauthors = Hayashi R, Wada H, Ito K, Adcock IM | title = Effects of glucocorticoids on gene transcription | journal = European Journal of Pharmacology | volume = 500 | issue = 1–3 | pages = 51–62 | date = outubro de 2004 | pmid = 15464020 | doi = 10.1016/j.ejphar.2004.07.011 }}</ref> que se describen máis abaixo.

=== Transactivación ===

Un mecanismo directo de acción implica a [[homodimerización]] do receptor, a translocación vía [[transporte activo]] ao [[núcleo celular]] e a unión a [[elemento de resposta ao ADN|elementos de resposta ao ADN]] específicos activadores da 
[[Transcrición (xenética)|transcrición]] de xenes. Este mecanismo de acción denomínase [[transactivación]]. A resposta biolóxica depende do tipo celular.<ref>Gaurang C. Patel; J. Cameron Millar; Abbot F. Clark. Glucocorticoid Receptor Transactivation Is Required for Glucocorticoid-Induced Ocular Hypertension and Glaucoma. Investigative Ophthalmology & Visual Science., maio de 2019, Vol.60, 1967-1978. doi:https://doi.org/10.1167/iovs.18-26383</ref>

=== Transrepresión ===
En ausencia de GCR activado, outros factores de transcrición como [[NF-κB]] ou [[AP-1 (factor de transcrición)|AP-1]] poden transactivar xenes diana.<ref name="pmid8290595">{{cite journal | vauthors = Ray A, Prefontaine KE | title = Physical association and functional antagonism between the p65 subunit of transcription factor NF-kappa B and the glucocorticoid receptor | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 91 | issue = 2 | pages = 752–756 | date = xaneiro de 1994 | pmid = 8290595 | pmc = 43027 | doi = 10.1073/pnas.91.2.752 | bibcode = 1994PNAS...91..752R }}</ref> Porén, o GCR activado pode formar complexos con estes outros [[factor de transcrición|factores de transcrición]] e impedirlles unirse aos seus xenes diana e así reprimir a expresión de xenes que normalmente son regulados á alza por NF-κB ou AP-1. Este mecanismo indirecto de acción denomínase [[transrepresión]].<ref name=Coutinho/> A transrepresión do GCR por medio de NF-κB e AP-1 está restrinxida a só certos tipos celulares e non se considera o mecanismo universal para a represión de IκBα (I kapaB alfa é unha proteína inhibidora que impide o transporte nuclear e activación do factor de transcrición NF-kapaB). <ref name=Coutinho>{{cite journal | vauthors = Coutinho AE, Chapman KE | title = The anti-inflammatory and immunosuppressive effects of glucocorticoids, recent developments and mechanistic insights | journal = Molecular and Cellular Endocrinology | volume = 335 | issue = 1 | pages = 2–13 | date = marzo de 2011 | pmid = 20398732 | pmc = 3047790 | doi = 10.1016/j.mce.2010.04.005 }}</ref><ref>{{cite journal | vauthors = Heck S, Bender K, Kullmann M, Göttlicher M, Herrlich P, Cato AC | title = I kappaB alpha-independent downregulation of NF-kappaB activity by glucocorticoid receptor | journal = The EMBO Journal | volume = 16 | issue = 15 | pages = 4698–4707 | date = agosto de 1997 | pmid = 9303314 | pmc = 1170096 | doi = 10.1093/emboj/16.15.4698 }}</ref>

== Importancia clínica ==
O GCR é anormal na [[resistencia a glicocorticoides|resistencia a glicocorticoides familiar]].<ref>{{cite journal | vauthors = Mendonca BB, Leite MV, de Castro M, Kino T, Elias LL, Bachega TA, Arnhold IJ, Chrousos GP, Latronico AC | display-authors = 6 | title = Female pseudohermaphroditism caused by a novel homozygous missense mutation of the GR gene | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 87 | issue = 4 | pages = 1805–1809 | date = abril de 2002 | pmid = 11932321 | doi = 10.1210/jcem.87.4.8379 }}</ref>

En estruturas do [[sistema nervioso central]], aumenta o interese polo receptor de glicocorticoides como novo representante da integración [[neuroendócrino|neuroendócrina]], funcionando como un compoñente importante da influencia endócrina (especificamente a resposta ao estrés) sobre o [[cerebro]]. O receptor está agora implicado en adaptacións a curto e longo prazo observadas en resposta a estresantes e pode ser fundamental para comprender trastornos psicolóxicos, como algúns ou todos os subtipos de [[depresión (psicoloxía)|depresión]] e [[trastorno por estrés postraumático]].<ref name="Maletic">{{cite journal | vauthors = Maletic V, Robinson M, Oakes T, Iyengar S, Ball SG, Russell J | title = Neurobiology of depression: an integrated view of key findings | journal = International Journal of Clinical Practice | volume = 61 | issue = 12 | pages = 2030–2040 | date = decembro de 2007 | pmid = 17944926 | pmc = 2228409 | doi = 10.1111/j.1742-1241.2007.01602.x }} [Texto completo libre]</ref> As observacións de longa duración como a desregulación do estado de ánimo típica da [[enfermidade de Cushing]] demostran o papel dos [[corticosteroide]]s na regulación do estado psicolóxico; avances recentes demostraron interaccións coa [[norepinefrina]] e [[serotonina]] a nivel neural.<ref name="Savitz">{{cite journal | vauthors = Savitz J, Lucki I, Drevets WC | title = 5-HT(1A) receptor function in major depressive disorder | journal = Progress in Neurobiology | volume = 88 | issue = 1 | pages = 17–31 | date = maio de 2009 | pmid = 19428959 | pmc = 2736801 | doi = 10.1016/j.pneurobio.2009.01.009 }} [Texto completo libre]</ref><ref>Schechter DS, Moser DA, Paoloni-Giacobino A, Stenz A, Gex-Fabry M, Aue T, Adouan W, Cordero MI, Suardi F, Manini A, Sancho Rossignol A, Merminod G, Ansermet F, Dayer AG, Rusconi Serpa S (epub May 29, 2015). Methylation of NR3C1 is related to maternal PTSD, parenting stress and maternal medial prefrontal cortical activity in response to child separation among mothers with histories of violence exposure. Frontiers in Psychology. http://www.frontiersin.org/Journal/Abstract.aspx?s=944&name=psychology_for_clinical_settings&ART_DOI=10.3389/fpsyg.2015.00690&field=&journalName=Frontiers_in_Psychology&id=139466</ref>

Na [[preeclampsia]] (un trastorno hipertensivo que pode ocorrer en mulleres xestantes), o nivel de secuencias de [[microARN]] que posiblemente teñen como diana esta proteína é elevado no [[sangue]] da nai. A [[placenta]] eleva o nivel de [[exosoma (vesícula)|exosomas]] que conteñen este microARN, o cal ten como resultado a inhibición da [[tradución de proteínas|tradución]] da molécula. A importancia clínica desta información aínda non está clara.<ref>{{cite journal | vauthors = Salomon C, Guanzon D, Scholz-Romero K, Longo S, Correa P, Illanes SE, Rice GE | title = Placental Exosomes as Early Biomarker of Preeclampsia: Potential Role of Exosomal MicroRNAs Across Gestation | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 102 | issue = 9 | pages = 3182–3194 | date = setembro de 2017 | pmid = 28531338 | doi = 10.1210/jc.2017-00672 }}</ref>

== Agonistas e antagonistas ==
A [[dexametasona]] e outros [[corticosteroide]]s son [[agonista]]s, mentres que a [[mifepristona]] e [[cetoconazol]] son [[antagonista de receptor|antagonistas]] do GCR. Os [[esteroide anabólico|esteroides anabólicos]] tamén impiden que o cortisol se una ao GCR.

== Interaccións ==
O receptor de glicocorticoides presenta [[intracción proteína-proteína|interaccións]] con:
{{div col|colwidth=20em}}
* [[BAG1]],<ref name="pmid9603979">{{cite journal | vauthors = Kullmann M, Schneikert J, Moll J, Heck S, Zeiner M, Gehring U, Cato AC | title = RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis | journal = The Journal of Biological Chemistry | volume = 273 | issue = 23 | pages = 14620–14625 | date = xuño de 1998 | pmid = 9603979 | doi = 10.1074/jbc.273.23.14620  }}</ref><ref name="pmid11101523">{{cite journal | vauthors = Schneikert J, Hübner S, Langer G, Petri T, Jäättelä M, Reed J, Cato AC | title = Hsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptor | journal = The EMBO Journal | volume = 19 | issue = 23 | pages = 6508–6516 | date = decembro de 2000 | pmid = 11101523 | pmc = 305849 | doi = 10.1093/emboj/19.23.6508 }}</ref>
* [[CEBPB]],<ref name="pmid9817600">{{cite journal | vauthors = Boruk M, Savory JG, Haché RJ | title = AF-2-dependent potentiation of CCAAT enhancer binding protein beta-mediated transcriptional activation by glucocorticoid receptor | journal = Molecular Endocrinology | volume = 12 | issue = 11 | pages = 1749–1763 | date = novembro de 1998 | pmid = 9817600 | doi = 10.1210/mend.12.11.0191 }}</ref>
* [[CREBBP]],<ref name="pmid9649342">{{cite journal | vauthors = Almlöf T, Wallberg AE, Gustafsson JA, Wright AP | title = Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau 1-core activation domain and target factors | journal = Biochemistry | volume = 37 | issue = 26 | pages = 9586–9594 | date = xuño de 1998 | pmid = 9649342 | doi = 10.1021/bi973029x }}</ref>
* [[DAP3]],<ref name="pmid10903152">{{cite journal | vauthors = Hulkko SM, Wakui H, Zilliacus J | title = The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function | journal = The Biochemical Journal | volume = 349 | issue = 3 | pages = 885–893 | date = agosto de 2000 | pmid = 10903152 | pmc = 1221218 | doi = 10.1042/bj3490885 | series = 349 }}</ref>
* [[DAXX]],<ref name="pmid12595526">{{cite journal | vauthors = Lin DY, Lai MZ, Ann DK, Shih HM | title = Promyelocytic leukemia protein (PML) functions as a glucocorticoid receptor co-activator by sequestering Daxx to the PML oncogenic domains (PODs) to enhance its transactivation potential | journal = The Journal of Biological Chemistry | volume = 278 | issue = 18 | pages = 15958–15965 | date = maio de 2003 | pmid = 12595526 | doi = 10.1074/jbc.M300387200  }}</ref>
* [[HSP90AA1]],<ref name=pmid10903152/><ref name="pmid10066374">{{cite journal | vauthors = Jibard N, Meng X, Leclerc P, Rajkowski K, Fortin D, Schweizer-Groyer G, Catelli MG, Baulieu EE, Cadepond F | display-authors = 6 | title = Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR) | journal = Experimental Cell Research | volume = 247 | issue = 2 | pages = 461–474 | date = marzo de 1999 | pmid = 10066374 | doi = 10.1006/excr.1998.4375 }}</ref><ref name="pmid12093808">{{cite journal | vauthors = Kanelakis KC, Shewach DS, Pratt WB | title = Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly | journal = The Journal of Biological Chemistry | volume = 277 | issue = 37 | pages = 33698–33703 | date = setembro de 2002 | pmid = 12093808 | doi = 10.1074/jbc.M204164200  }}</ref><ref name="pmid9334248">{{cite journal | vauthors = Hecht K, Carlstedt-Duke J, Stierna P, Gustafsson J, Brönnegârd M, Wikström AC | title = Evidence that the beta-isoform of the human glucocorticoid receptor does not act as a physiologically significant repressor | journal = The Journal of Biological Chemistry | volume = 272 | issue = 42 | pages = 26659–26664 | date = outubro de 1997 | pmid = 9334248 | doi = 10.1074/jbc.272.42.26659 }}</ref><ref name="pmid8898375">{{cite journal | vauthors = de Castro M, Elliot S, Kino T, Bamberger C, Karl M, Webster E, Chrousos GP | title = The non-ligand binding beta-isoform of the human glucocorticoid receptor (hGR beta): tissue levels, mechanism of action, and potential physiologic role | journal = Molecular Medicine | volume = 2 | issue = 5 | pages = 597–607 | date = setembro de 1996 | pmid = 8898375 | pmc = 2230188 | doi = 10.1007/BF03401643 }}</ref><ref name="pmid8645634">{{cite journal | vauthors = van den Berg JD, Smets LA, van Rooij H | title = Agonist-free transformation of the glucocorticoid receptor in human B-lymphoma cells | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 57 | issue = 3–4 | pages = 239–249 | date = febreiro de 1996 | pmid = 8645634 | doi = 10.1016/0960-0760(95)00271-5  }}</ref><ref name="pmid8621522">{{cite journal | vauthors = Stancato LF, Silverstein AM, Gitler C, Groner B, Pratt WB | title = Use of the thiol-specific derivatizing agent N-iodoacetyl-3-[125I]iodotyrosine to demonstrate conformational differences between the unbound and hsp90-bound glucocorticoid receptor hormone binding domain | journal = The Journal of Biological Chemistry | volume = 271 | issue = 15 | pages = 8831–8836 | date = abril de 1996 | pmid = 8621522 | doi = 10.1074/jbc.271.15.8831  }}</ref>
* [[HNRPU]],<ref name="pmid9353307">{{cite journal | vauthors = Eggert M, Michel J, Schneider S, Bornfleth H, Baniahmad A, Fackelmayer FO, Schmidt S, Renkawitz R | display-authors = 6 | title = The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U | journal = The Journal of Biological Chemistry | volume = 272 | issue = 45 | pages = 28471–28478 | date = novembro de 1997 | pmid = 9353307 | doi = 10.1074/jbc.272.45.28471  }}</ref>
* [[MED1]],<ref name=pmid11266503/><ref name=pmid10508170/>
* [[MED14]],<ref name="pmid10508170">{{cite journal | vauthors = Hittelman AB, Burakov D, Iñiguez-Lluhí JA, Freedman LP, Garabedian MJ | title = Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins | journal = The EMBO Journal | volume = 18 | issue = 19 | pages = 5380–5388 | date = outubro de 1999 | pmid = 10508170 | pmc = 1171607 | doi = 10.1093/emboj/18.19.5380 }}</ref>
* [[Receptor de mineralocorticoides]],<ref name="pmid11154266">{{cite journal | vauthors = Savory JG, Préfontaine GG, Lamprecht C, Liao M, Walther RF, Lefebvre YA, Haché RJ | title = Glucocorticoid receptor homodimers and glucocorticoid-mineralocorticoid receptor heterodimers form in the cytoplasm through alternative dimerization interfaces | journal = Molecular and Cellular Biology | volume = 21 | issue = 3 | pages = 781–793 | date = febreiro de 2001 | pmid = 11154266 | pmc = 86670 | doi = 10.1128/MCB.21.3.781-793.2001 }}</ref>
* [[NRIP1]],<ref name=pmid11266503/><ref name="pmid12773562">{{cite journal | vauthors = Tazawa H, Osman W, Shoji Y, Treuter E, Gustafsson JA, Zilliacus J | title = Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140 | journal = Molecular and Cellular Biology | volume = 23 | issue = 12 | pages = 4187–4198 | date = xuño de 2003 | pmid = 12773562 | pmc = 156128 | doi = 10.1128/MCB.23.12.4187-4198.2003 }}</ref><ref name="pmid10364267">{{cite journal | vauthors = Subramaniam N, Treuter E, Okret S | title = Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids | journal = The Journal of Biological Chemistry | volume = 274 | issue = 25 | pages = 18121–18127 | date = xuño de 1999 | pmid = 10364267 | doi = 10.1074/jbc.274.25.18121  }}</ref>
* [[NCOR1]],<ref name="pmid12569182">{{cite journal | vauthors = Stevens A, Garside H, Berry A, Waters C, White A, Ray D | title = Dissociation of steroid receptor coactivator 1 and nuclear receptor corepressor recruitment to the human glucocorticoid receptor by modification of the ligand-receptor interface: the role of tyrosine 735 | journal = Molecular Endocrinology | volume = 17 | issue = 5 | pages = 845–859 | date = maio de 2003 | pmid = 12569182 | doi = 10.1210/me.2002-0320  }}</ref><ref name="pmid12011091">{{cite journal | vauthors = Schulz M, Eggert M, Baniahmad A, Dostert A, Heinzel T, Renkawitz R | title = RU486-induced glucocorticoid receptor agonism is controlled by the receptor N terminus and by corepressor binding | journal = The Journal of Biological Chemistry | volume = 277 | issue = 29 | pages = 26238–26243 | date = July 2002 | pmid = 12011091 | doi = 10.1074/jbc.M203268200  }}</ref>
* [[NCOA1]],<ref name=pmid11266503/><ref name="pmid12118039">{{cite journal | vauthors = Kucera T, Waltner-Law M, Scott DK, Prasad R, Granner DK | title = A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 29 | pages = 26098–26102 | date = xullo de 2002 | pmid = 12118039 | doi = 10.1074/jbc.M204013200 }}</ref>
* [[NCOA2]],<ref name="pmid11266503">{{cite journal | vauthors = Zilliacus J, Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson JA | title = Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140 | journal = Molecular Endocrinology | volume = 15 | issue = 4 | pages = 501–511 | date = abril de 2001 | pmid = 11266503 | doi = 10.1210/mend.15.4.0624 }}</ref><ref name="pmid12151000">{{cite journal | vauthors = Bledsoe RK, Montana VG, Stanley TB, Delves CJ, Apolito CJ, McKee DD, Consler TG, Parks DJ, Stewart EL, Willson TM, Lambert MH, Moore JT, Pearce KH, Xu HE | display-authors = 6 | title = Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition | journal = Cell | volume = 110 | issue = 1 | pages = 93–105 | date = xullo de 2002 | pmid = 12151000 | doi = 10.1016/S0092-8674(02)00817-6 }}</ref>
* [[NCOA3]],<ref name=pmid11266503/><ref name="pmid12917342">{{cite journal | vauthors = Hsiao PW, Fryer CJ, Trotter KW, Wang W, Archer TK | title = BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation | journal = Molecular and Cellular Biology | volume = 23 | issue = 17 | pages = 6210–6220 | date = setembro de 2003 | pmid = 12917342 | pmc = 180928 | doi = 10.1128/MCB.23.17.6210-6220.2003 }}</ref>
* [[POU2F1]],<ref name=pmid10480874>{{cite journal | vauthors = Préfontaine GG, Walther R, Giffin W, Lemieux ME, Pope L, Haché RJ | title = Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter | journal = The Journal of Biological Chemistry | volume = 274 | issue = 38 | pages = 26713–26719 | date = setembro 1999 | pmid = 10480874 | doi = 10.1074/jbc.274.38.26713  }}</ref><ref name="pmid9584182">{{cite journal | vauthors = Préfontaine GG, Lemieux ME, Giffin W, Schild-Poulter C, Pope L, LaCasse E, Walker P, Haché RJ | display-authors = 6 | title = Recruitment of octamer transcription factors to DNA by glucocorticoid receptor | journal = Molecular and Cellular Biology | volume = 18 | issue = 6 | pages = 3416–3430 | date = xuño de 1998 | pmid = 9584182 | pmc = 108923 | doi = 10.1128/MCB.18.6.3416 }}</ref>
* [[RANBP9]],<ref name=pmid12361945>{{cite journal | vauthors = Rao MA, Cheng H, Quayle AN, Nishitani H, Nelson CC, Rennie PS | title = RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor | journal = The Journal of Biological Chemistry | volume = 277 | issue = 50 | pages = 48020–48027 | date = decembro de 2002 | pmid = 12361945 | doi = 10.1074/jbc.M209741200 }}</ref>
* [[RELA]],<ref name="pmid12361945" /><ref name="pmid10995388">{{cite journal | vauthors = Nissen RM, Yamamoto KR | title = The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain | journal = Genes & Development | volume = 14 | issue = 18 | pages = 2314–2329 | date = setembro de 2000 | pmid = 10995388 | pmc = 316928 | doi = 10.1101/gad.827900 }}</ref><ref name="pmid7659084">{{cite journal | vauthors = Caldenhoven E, Liden J, Wissink S, Van de Stolpe A, Raaijmakers J, Koenderman L, Okret S, Gustafsson JA, Van der Saag PT | display-authors = 6 | title = Negative cross-talk between RelA and the glucocorticoid receptor: a possible mechanism for the antiinflammatory action of glucocorticoids | journal = Molecular Endocrinology | volume = 9 | issue = 4 | pages = 401–412 | date = abril de 1995 | pmid = 7659084 | doi = 10.1210/mend.9.4.7659084 }}</ref>
* [[SMAD3]],<ref name="pmid12902338">{{cite journal | vauthors = Li G, Wang S, Gelehrter TD | title = Identification of glucocorticoid receptor domains involved in transrepression of transforming growth factor-beta action | journal = The Journal of Biological Chemistry | volume = 278 | issue = 43 | pages = 41779–41788 | date = outubro de 2003 | pmid = 12902338 | doi = 10.1074/jbc.M305350200  }}</ref><ref name="pmid10518526">{{cite journal | vauthors = Song CZ, Tian X, Gelehrter TD | title = Glucocorticoid receptor inhibits transforming growth factor-beta signaling by directly targeting the transcriptional activation function of Smad3 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 21 | pages = 11776–11781 | date = outubro de 1999 | pmid = 10518526 | pmc = 18362 | doi = 10.1073/pnas.96.21.11776  | bibcode = 1999PNAS...9611776S }}</ref>
* [[SMARCD1]],<ref name=pmid12917342/>
* [[SMARCA4]]<ref name=pmid12917342/><ref name="pmid10688647">{{cite journal | vauthors = Wallberg AE, Neely KE, Hassan AH, Gustafsson JA, Workman JL, Wright AP | title = Recruitment of the SWI-SNF chromatin remodeling complex as a mechanism of gene activation by the glucocorticoid receptor tau1 activation domain | journal = Molecular and Cellular Biology | volume = 20 | issue = 6 | pages = 2004–2013 | date = marzo de 2000 | pmid = 10688647 | pmc = 110817 | doi = 10.1128/MCB.20.6.2004-2013.2000 }}</ref>
* [[STAT3]],<ref name="pmid14522952">{{cite journal | vauthors = Lerner L, Henriksen MA, Zhang X, Darnell JE | title = STAT3-dependent enhanceosome assembly and disassembly: synergy with GR for full transcriptional increase of the alpha 2-macroglobulin gene | journal = Genes & Development | volume = 17 | issue = 20 | pages = 2564–2577 | date = outubro de 2003 | pmid = 14522952 | pmc = 218150 | doi = 10.1101/gad.1135003 }}</ref><ref name="pmid9388192">{{cite journal | vauthors = Zhang Z, Jones S, Hagood JS, Fuentes NL, Fuller GM | title = STAT3 acts as a co-activator of glucocorticoid receptor signaling | journal = The Journal of Biological Chemistry | volume = 272 | issue = 49 | pages = 30607–30610 | date = decembro de 1997 | pmid = 9388192 | doi = 10.1074/jbc.272.49.30607  }}</ref>
* [[STAT5B]],<ref name="pmid8878484">{{cite journal | vauthors = Stöcklin E, Wissler M, Gouilleux F, Groner B | title = Functional interactions between Stat5 and the glucocorticoid receptor | journal = Nature | volume = 383 | issue = 6602 | pages = 726–728 | date = outubro de 1996 | pmid = 8878484 | doi = 10.1038/383726a0 | bibcode = 1996Natur.383..726S | url = https://hal-univ-tours.archives-ouvertes.fr/hal-02427426/file/Functional%20interactions%20between%20StatS%20and%20GR.pdf }}</ref>
* [[Tiorredoxina]],<ref name="pmid9915858">{{cite journal | vauthors = Makino Y, Yoshikawa N, Okamoto K, Hirota K, Yodoi J, Makino I, Tanaka H | title = Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function | journal = The Journal of Biological Chemistry | volume = 274 | issue = 5 | pages = 3182–3188 | date = xaneiro de 1999 | pmid = 9915858 | doi = 10.1074/jbc.274.5.3182 }}</ref>
* [[TRIM28]],<ref name="pmid9742105">{{cite journal | vauthors = Chang CJ, Chen YL, Lee SC | title = Coactivator TIF1beta interacts with transcription factor C/EBPbeta and glucocorticoid receptor to induce alpha1-acid glycoprotein gene expression | journal = Molecular and Cellular Biology | volume = 18 | issue = 10 | pages = 5880–5887 | date = outubro de 1998 | pmid = 9742105 | pmc = 109174 | doi = 10.1128/mcb.18.10.5880 }}</ref> e
* [[YWHAH]].<ref name="pmid9079630">{{cite journal | vauthors = Wakui H, Wright AP, Gustafsson J, Zilliacus J | title = Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein | journal = The Journal of Biological Chemistry | volume = 272 | issue = 13 | pages = 8153–8156 | date = marzo de 1997 | pmid = 9079630 | doi = 10.1074/jbc.272.13.8153  }}</ref>
{{Div col end}}

== Notas ==
{{listaref|2}}

== Véxase tamén ==
=== Outros artigos ===
* [[Receptor de glicocorticoides de membrana]]
* [[Agonista do receptor de glicocorticoides selectivo]] (SEGRA)

=== Bibliografía ===
{{refempeza | 2}}
* {{cite journal | vauthors = Adcock IM, Ito K | title = Molecular mechanisms of corticosteroid actions | journal = Monaldi Archives for Chest Disease = Archivio Monaldi per le Malattie del Torace | volume = 55 | issue = 3 | pages = 256–266 | date = xuño de 2000 | pmid = 10948677 }}
* {{cite journal | vauthors = Chikanza IC | title = Mechanisms of corticosteroid resistance in rheumatoid arthritis: a putative role for the corticosteroid receptor beta isoform | journal = Annals of the New York Academy of Sciences | volume = 966 | issue = 1 | pages = 39–48 | date = xuño de 2002 | pmid = 12114257 | doi = 10.1111/j.1749-6632.2002.tb04200.x | bibcode = 2002NYASA.966...39C }}
* {{cite journal | vauthors = Neeck G, Kluter A, Dotzlaw H, Eggert M | title = Involvement of the glucocorticoid receptor in the pathogenesis of rheumatoid arthritis | journal = Annals of the New York Academy of Sciences | volume = 966 | issue = 1 | pages = 491–495 | date = xuño de 2002 | pmid = 12114309 | doi = 10.1111/j.1749-6632.2002.tb04252.x | bibcode = 2002NYASA.966..491N }}
* {{cite journal | vauthors = Yudt MR, Cidlowski JA | title = The glucocorticoid receptor: coding a diversity of proteins and responses through a single gene | journal = Molecular Endocrinology | volume = 16 | issue = 8 | pages = 1719–1726 | date = agosto de 2002 | pmid = 12145329 | doi = 10.1210/me.2002-0106  }}
* {{cite journal | vauthors = Torrego A, Pujols L, Picado C | title = [Response to glucocorticoid treatment in asthma. The role of alpha and beta isoforms of the glucocorticoid receptor] | journal = Archivos de Bronconeumologia | volume = 38 | issue = 9 | pages = 436–440 | date = September 2002 | pmid = 12237016 | doi = 10.1016/S0300-2896(02)75258-7 }}
* {{cite journal | vauthors = Bray PJ, Cotton RG | title = Variations of the human glucocorticoid receptor gene (NR3C1): pathological and in vitro mutations and polymorphisms | journal = Human Mutation | volume = 21 | issue = 6 | pages = 557–568 | date = xuño de 2003 | pmid = 12754700 | doi = 10.1002/humu.10213 }}
* {{cite journal | vauthors = Kino T, Pavlakis GN | title = Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1 | journal = DNA and Cell Biology | volume = 23 | issue = 4 | pages = 193–205 | date = abril de 2004 | pmid = 15142377 | doi = 10.1089/104454904773819789 | url = https://zenodo.org/record/1235217 }}
* {{cite journal | vauthors = Lu NZ, Cidlowski JA | title = The origin and functions of multiple human glucocorticoid receptor isoforms | journal = Annals of the New York Academy of Sciences | volume = 1024 | issue = 1 | pages = 102–123 | date = xuño de 2004 | pmid = 15265776 | doi = 10.1196/annals.1321.008  | bibcode = 2004NYASA1024..102L | url = https://zenodo.org/record/1235886 }}
* {{cite journal | vauthors = Kino T, Chrousos GP | title = Human immunodeficiency virus type-1 accessory protein Vpr: a causative agent of the AIDS-related insulin resistance/lipodystrophy syndrome? | journal = Annals of the New York Academy of Sciences | volume = 1024 | issue = 1 | pages = 153–167 | date = xuño de 2004 | pmid = 15265780 | doi = 10.1196/annals.1321.013  | bibcode = 2004NYASA1024..153K | url = https://zenodo.org/record/1235880 }}
* {{cite journal | vauthors = Andersen JL, Planelles V | title = The role of Vpr in HIV-1 pathogenesis | journal = Current HIV Research | volume = 3 | issue = 1 | pages = 43–51 | date = xaneiro de 2005 | pmid = 15638722 | doi = 10.2174/1570162052772988 }}
* {{cite journal | vauthors = Le Rouzic E, Benichou S | title = The Vpr protein from HIV-1: distinct roles along the viral life cycle | journal = Retrovirology | volume = 2 | issue = 1 | pages = 11 | date = febreiro de 2005 | pmid = 15725353 | pmc = 554975 | doi = 10.1186/1742-4690-2-11 }}
* {{cite journal | vauthors = Muthumani K, Choo AY, Premkumar A, Hwang DS, Thieu KP, Desai BM, Weiner DB | title = Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism | journal = Cell Death and Differentiation | volume = 12 | issue = Suppl 1 | pages = 962–970 | date = agosto de 2005 | pmid = 15832179 | doi = 10.1038/sj.cdd.4401583  }}
* {{cite journal | vauthors = Zhou J, Cidlowski JA | title = The human glucocorticoid receptor: one gene, multiple proteins and diverse responses | journal = Steroids | volume = 70 | issue = 5–7 | pages = 407–417 | year = 2005 | pmid = 15862824 | doi = 10.1016/j.steroids.2005.02.006  | url = https://zenodo.org/record/1259367 }}
* {{cite journal | vauthors = Chrousos GP, Kino T | title = Intracellular glucocorticoid signaling: a formerly simple system turns stochastic | journal = Science's STKE | volume = 2005 | issue = 304 | pages = pe48 | date = outubro de 2005 | pmid = 16204701 | doi = 10.1126/stke.3042005pe48  }}
* {{cite journal | vauthors = Plotkin LL, Labutin AL, Lebedev LV, Khanukov LA, Zelikson OS | title = [Balloon probe for the removal of emboli and thrombi] | journal = Meditsinskaya Tekhnika | issue = 3 | pages = 42–43 | year = 1975 | pmid = 1152650 }}
* {{cite journal | vauthors = Subramaniam M, Colvard D, Keeting PE, Rasmussen K, Riggs BL, Spelsberg TC | title = Glucocorticoid regulation of alkaline phosphatase, osteocalcin, and proto-oncogenes in normal human osteoblast-like cells | journal = Journal of Cellular Biochemistry | volume = 50 | issue = 4 | pages = 411–424 | date = decembro de 1992 | pmid = 1469072 | doi = 10.1002/jcb.240500410  }}
* {{cite journal | vauthors = Scherrer LC, Pratt WB | title = Association of the transformed glucocorticoid receptor with a cytoskeletal protein complex | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 41 | issue = 3–8 | pages = 719–721 | date = marzo de 1992 | pmid = 1562545 | doi = 10.1016/0960-0760(92)90411-B  }}
* {{cite journal | vauthors = Cadepond F, Gasc JM, Delahaye F, Jibard N, Schweizer-Groyer G, Segard-Maurel I, Evans R, Baulieu EE | display-authors = 6 | title = Hormonal regulation of the nuclear localization signals of the human glucocorticosteroid receptor | journal = Experimental Cell Research | volume = 201 | issue = 1 | pages = 99–108 | date = xullo de 1992 | pmid = 1612132 | doi = 10.1016/0014-4827(92)90352-9 }}
* {{cite journal | vauthors = Hurley DM, Accili D, Stratakis CA, Karl M, Vamvakopoulos N, Rorer E, Constantine K, Taylor SI, Chrousos GP | display-authors = 6 | title = Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance | journal = The Journal of Clinical Investigation | volume = 87 | issue = 2 | pages = 680–686 | date = febreiro de 1991 | pmid = 1704018 | pmc = 296359 | doi = 10.1172/JCI115046 }}
* {{cite journal | vauthors = Encío IJ, Detera-Wadleigh SD | title = The genomic structure of the human glucocorticoid receptor | journal = The Journal of Biological Chemistry | volume = 266 | issue = 11 | pages = 7182–7188 | date = abril de 1991 | pmid = 1707881 | doi = 10.1016/S0021-9258(20)89627-6  }}
{{reftermina}}

=== Ligazóns externas ===
* [http://www.hprd.org/protein/00679 Human Protein Reference Database] {{Webarchive|url=https://web.archive.org/web/20060301010038/http://www.hprd.org/protein/00679 |date=2006-03-01 }}
* {{MeshName|Glucocorticoid+receptors}}
* {{PDBe-KB2|P04150|Glucocorticoid receptor}}

{{control de autoridades}}

[[Categoría:Proxectos xenoma]]
[[Categoría:Receptores nucleares]]