Просмотр кода страницы Глюкокортикоидный рецептор

{{protein
|name=nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor)
|caption=
|image=
|width=
|HGNCid=7978
|Symbol=NR3C1
|AltSymbols=GRL
|EntrezGene=
|OMIM=138040
|RefSeq=NM_000176
|UniProt=P04150
|PDB=
|ECnumber=
|Chromosome=5
|Arm=q
|Band=31
|LocusSupplementaryData=
}}
'''Глюкокортикоидный рецептор''' ({{lang-en|GR}}), также известный как '''NR3C1'''  — белок [[человек]]а, рецептор [[глюкокортикоид]]ов и [[фактор транскрипции]]. Относится к [[Ядерные рецепторы|ядерным рецепторам]], что отражено в названии ({{lang-en|nuclear receptor subfamily 3, group C, member 1}}, '''NR3C1''').

[[Альтернативный сплайсинг]] порождает три изоформы рецептора: альфа, бета<ref name="pmid8621628">{{публикация|статья |заглавие=The human glucocorticoid receptor beta isoform. Expression, biochemical properties, and putative function |издание=[[Journal of Biological Chemistry]] |volume=271 |issue=16 |pages=9550—9559 |pmid=8621628 |ссылка=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=8621628 |язык=en |автор=Oakley |автор имя=R. H. |автор2=Sar |автор2 имя=M. |автор3=Cidlowski |автор3 имя=J. A. |месяц=04 |год=1996 |doi=10.1074/jbc.271.16.9550 }}</ref> и гамма<ref name="pmid10566686">{{публикация|статья |заглавие=Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing |издание={{Нп3|Journal of Clinical Endocrinology and Metabolism}} |volume=84 |issue=11 |pages=4283—4286 |pmid=10566686 |ссылка=http://jcem.endojournals.org/cgi/pmidlookup?view=long&pmid=10566686 |язык=en |автор=Rivers |автор имя=C. |автор2=Levy |автор2 имя=A. |автор3=Hancock |автор3 имя=J. |автор4=Lightman |автор4 имя=S. |автор5=Norman |автор5 имя=M. |месяц=11 |год=1999 |doi=10.1210/jcem.84.11.6235 }}</ref>.

GR [[Экспрессия генов|экспрессируется]] почти в каждой клетке организма и регулирует [[ген]]ы, контролирующие развитие, [[метаболизм]] и [[иммунный ответ]]. Поскольку ген рецептора экспрессируется в нескольких формах, он оказывает множество различных ([[Плейотропия|плейотропных]]) эффектов в разных частях тела.

Когда [[глюкокортикоиды]] связываются с GR, основной механизм их действия заключается в регуляции [[Транскрипция (биология)|транскрипции]] генов<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 = December 2006 | pmid = 17132855 | doi = 10.1124/pr.58.4.9 | s2cid = 28626145 }} [Free full text]</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 = October 2005 | pmid = 16236742 | doi = 10.1056/NEJMra050541 | s2cid = 5744727 }}</ref>. Несвязанный рецептор находится в [[Цитозоль|цитозоле]] клетки. После связывания рецептора с глюкокортикоидом комплекс рецептор-глюкокортикоид может пойти по одному из двух путей. Активированный комплекс GR повышает экспрессию противовоспалительных белков в [[клеточное ядро|ядре]] или подавляет экспрессию провоспалительных белков в цитозоле (предотвращая транслокацию других [[Факторы транскрипции|факторов транскрипции]] из цитозоля в ядро).

У человека ген, кодирующий глюкокортикоидный рецептор — ''[https://www.genecards.org/cgi-bin/carddisp.pl?gene=NR3C1 NR3C1]'', локализован на длинном плече (q-плече) [[5-я хромосома человека|5-й хромосомы]]<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 = December 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 = May 1989 | pmid = 2744768 | doi = 10.1016/0888-7543(89)90287-5 }}</ref>.

== Структура ==
Как и другие [[стероидные рецепторы]]<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 = May 1999 | pmid = 10406480 | doi = 10.1016/S0039-128X(99)00014-8 | s2cid = 18333397 }}</ref>, глюкокортикоидный рецептор имеет модульную структуру<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 = April 2005 | pmid = 15876404 | doi = 10.1016/j.jsbmb.2004.12.046 | s2cid = 25315991 }}</ref> и содержит следующие [[Домен белка|домен]]ы (обозначены A - F):

* A/B — N-концевой регуляторный домен
* C — ДНК-связывающий домен (DBD)
* D — шарнирная область
* E — лиганд-связывающий домен (LBD)
* F — С-концевой домен.

== Связывание лиганда и ответная реакция ==
В отсутствие гормона глюкокортикоидный рецептор (GR) находится в цитозоле в комплексе с различными белками, включая белок [[Hsp90|теплового шока 90]] (hsp90), белок теплового шока 70 (hsp70) и белок [[FKBP4]] (FK506-связывающий белок 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>. Эндогенный глюкокортикоидный гормон [[кортизол]] диффундирует через [[Клеточная мембрана|клеточную мембрану]] в цитоплазму и связывается с глюкокортикоидным рецептором (GR), что приводит к высвобождению [[Белки теплового шока|белков теплового шока]]. Образовавшаяся активированная форма GR имеет два основных механизма действия — трансактивацию и трансрепрессию<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 = January 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 = October 2004 | pmid = 15464020 | doi = 10.1016/j.ejphar.2004.07.011 }}</ref>, описанные ниже.

=== Трансактивация ===
Прямой механизм действия включает гомодимеризацию рецептора, транслокацию посредством активного транспорта в [[клеточное ядро]] и связывание со специфическими [[Элемент отклика гормона|чувствительными элементами ДНК]], активирующими [[Транскрипция (биология)|транскрипцию]] генов. Этот механизм действия называется трансактивацией.

=== Трансрепрессия ===
В отсутствие активированного GR другие [[Факторы транскрипции|транскрипционные факторы]], такие как NF-κB или AP-1, сами способны трансактивировать гены-мишени<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 = January 1994 | pmid = 8290595 | pmc = 43027 | doi = 10.1073/pnas.91.2.752 | doi-access = free | bibcode = 1994PNAS...91..752R }}</ref>. Однако активированный GR может вступать в комплекс с этими другими транскрипционными факторами и препятствовать их связыванию с генами-мишенями, что приводит к подавлению [[Экспрессия генов|экспрессии генов]], которые обычно повышаются [[NF-κB]] или AP-1. Этот непрямой механизм действия называется трансрепрессией. Трансрепрессия GR через NF-κB и [[AP-1 (транскрипционный фактор)|AP-1]] ограничена только определёнными типами клеток и не считается универсальным механизмом репрессии IκBα<ref>{{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 = March 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 = August 1997 | pmid = 9303314 | pmc = 1170096 | doi = 10.1093/emboj/16.15.4698 }}</ref>.

== Клиническое значение ==
GR аномален при семейной глюкокортикоидной резистентности<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 = April 2002 | pmid = 11932321 | doi = 10.1210/jcem.87.4.8379 | doi-access = free }}</ref>.

В структурах [[Центральная нервная система|центральной нервной системы]] глюкокортикоидный рецептор вызывает всё больший интерес как новый представитель нейроэндокринной интеграции, функционирующий в качестве основного компонента эндокринного влияния — в частности, стрессового ответа — на мозг. В настоящее время рецептор участвует как в краткосрочных, так и в долгосрочных адаптациях в ответ на стресс и может иметь решающее значение для понимания психологических расстройств, включая некоторые или все подтипы [[Депрессия|депрессии]] и [[Комплексное посттравматическое стрессовое расстройство|посттравматического стрессового расстройства]] (ПТСР)<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 = December 2007 | pmid = 17944926 | pmc = 2228409 | doi = 10.1111/j.1742-1241.2007.01602.x }} [Free full text]</ref>. Действительно, давние наблюдения, такие как дисрегуляции настроения, характерные для [[Болезнь Иценко — Кушинга|болезни Кушинга]], демонстрируют роль кортикостероидов в регуляции психологического состояния; последние достижения показали взаимодействие с [[норадреналин]]ом и [[серотонин]]ом на нейронном уровне<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 = May 2009 | pmid = 19428959 | pmc = 2736801 | doi = 10.1016/j.pneurobio.2009.01.009 }} [Free full text]</ref><ref name="pmid26074844">{{cite journal | vauthors = Schechter DS, Moser DA, Paoloni-Giacobino A, Stenz L, 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 |display-authors = 6| title = 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 | journal = Front Psychol | volume = 6 | issue = | pages = 690 | date = 2015 | pmid = 26074844 | pmc = 4447998 | doi = 10.3389/fpsyg.2015.00690 |doi-access = free}}</ref>.

При [[Преэклампсия|преэклампсии]] (гипертоническом заболевании, часто встречающемся у беременных женщин) в крови матери повышается уровень последовательности [[миРНК]], возможно, нацеленной на этот белок. Скорее, в плаценте повышается уровень [[Экзосомы|экзосом]], содержащих эту миРНК, что может привести к ингибированию [[Трансляция (биология)|трансляции]] молекулы. Клиническое значение этой информации пока не выяснено<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 = September 2017 | pmid = 28531338 | doi = 10.1210/jc.2017-00672 | doi-access = free }}</ref>.

==Взаимодействия==
Глюкокортикоидный рецептор [[Белок-белковые взаимодействия|взаимодействует]] с:
{{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 = J. Biol. Chem. | volume = 273 | issue = 23 | pages = 14620–5 |date=June 1998 | pmid = 9603979 | doi = 10.1074/jbc.273.23.14620 | doi-access = free }}</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 = EMBO J. | volume = 19 | issue = 23 | pages = 6508–16 |date=December 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 = Mol. Endocrinol. | volume = 12 | issue = 11 | pages = 1749–63 |date=November 1998 | pmid = 9817600 | doi = 10.1210/mend.12.11.0191 | doi-access = free }}</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 = 9586–94 |date=June 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 = Biochem. J. | volume = Pt 3 | issue = 3| pages = 885–93 |date=August 2000 | series = 349  | pmid = 10903152 | pmc = 1221218 | doi = 10.1042/bj3490885}}</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 = J. Biol. Chem. | volume = 278 | issue = 18 | pages = 15958–65 |date=May 2003 | pmid = 12595526 | doi = 10.1074/jbc.M300387200 | doi-access = free }}</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 | title = Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR) | journal = Exp. Cell Res. | volume = 247 | issue = 2 | pages = 461–74 |date=March 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 = J. Biol. Chem. | volume = 277 | issue = 37 | pages = 33698–703 |date=September 2002 | pmid = 12093808 | doi = 10.1074/jbc.M204164200 | doi-access = free }}</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 = J. Biol. Chem. | volume = 272 | issue = 42 | pages = 26659–64 |date=October 1997 | pmid = 9334248 | doi = 10.1074/jbc.272.42.26659 | doi-access = free }}</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 = Mol. Med. | volume = 2 | issue = 5 | pages = 597–607 |date=September 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 = J. Steroid Biochem. Mol. Biol. | volume = 57 | issue = 3–4 | pages = 239–49 |date=February 1996 | pmid = 8645634 | doi = 10.1016/0960-0760(95)00271-5 | s2cid = 20582144 }}</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 = J. Biol. Chem. | volume = 271 | issue = 15 | pages = 8831–6 |date=April 1996 | pmid = 8621522 | doi = 10.1074/jbc.271.15.8831 | doi-access = free }}</ref>
* [[HNRPU]],<ref name="pmid9353307">{{cite journal |vauthors=Eggert M, Michel J, Schneider S, Bornfleth H, Baniahmad A, Fackelmayer FO, Schmidt S, Renkawitz R | title = The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U | journal = J. Biol. Chem. | volume = 272 | issue = 45 | pages = 28471–8 |date=November 1997 | pmid = 9353307 | doi = 10.1074/jbc.272.45.28471 | doi-access = free }}</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 = EMBO J. | volume = 18 | issue = 19 | pages = 5380–8 |date=October 1999 | pmid = 10508170 | pmc = 1171607 | doi = 10.1093/emboj/18.19.5380 }}</ref>
* [[NR3C2]],<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 |url=https://archive.org/details/sim_molecular-and-cellular-biology_2001-02_21_3/page/781 | journal = Mol. Cell. Biol. | volume = 21 | issue = 3 | pages = 781–93 |date=February 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 |url=https://archive.org/details/sim_molecular-and-cellular-biology_2003-06_23_12/page/4187 | journal = Mol. Cell. Biol. | volume = 23 | issue = 12 | pages = 4187–98 |date=June 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 = J. Biol. Chem. | volume = 274 | issue = 25 | pages = 18121–7 |date=June 1999 | pmid = 10364267 | doi = 10.1074/jbc.274.25.18121 | doi-access = free }}</ref>
* [[Корепрессор ядерного рецептора 1|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 = Mol. Endocrinol. | volume = 17 | issue = 5 | pages = 845–59 |date=May 2003 | pmid = 12569182 | doi = 10.1210/me.2002-0320 | doi-access = free }}</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 = J. Biol. Chem. | volume = 277 | issue = 29 | pages = 26238–43 |date=July 2002 | pmid = 12011091 | doi = 10.1074/jbc.M203268200 | doi-access = free }}</ref>
* [[коактиватор ядерного рецептора 1|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 = J. Biol. Chem. | volume = 277 | issue = 29 | pages = 26098–102 |date=July 2002 | pmid = 12118039 | doi = 10.1074/jbc.M204013200 | doi-access = free }}</ref>
* [[коактиватор ядерного рецептора 2|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 = Mol. Endocrinol. | volume = 15 | issue = 4 | pages = 501–11 |date=April 2001 | pmid = 11266503 | doi = 10.1210/mend.15.4.0624 | doi-access = free }}</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 | 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=July 2002 | pmid = 12151000 | doi = 10.1016/S0092-8674(02)00817-6 | s2cid = 6955342 | doi-access = free }}</ref>
* [[коактиватор ядерного рецептора 3|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 |url=https://archive.org/details/sim_molecular-and-cellular-biology_2003-09_23_17/page/6210 | journal = Mol. Cell. Biol. | volume = 23 | issue = 17 | pages = 6210–20 |date=September 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 = 26713–9 | date = September 1999 | pmid = 10480874 | doi = 10.1074/jbc.274.38.26713 | doi-access = free }}</ref><ref name="pmid9584182">{{cite journal | vauthors = Préfontaine GG, Lemieux ME, Giffin W, Schild-Poulter C, Pope L, LaCasse E, Walker P, Haché RJ | title = Recruitment of octamer transcription factors to DNA by glucocorticoid receptor | url = https://archive.org/details/sim_molecular-and-cellular-biology_1998-06_18_6/page/3416 | journal = Molecular and Cellular Biology | volume = 18 | issue = 6 | pages = 3416–30 | date = June 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 = 48020–7 | date = December 2002 | pmid = 12361945 | doi = 10.1074/jbc.M209741200 | doi-access = free }}</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 Dev. | volume = 14 | issue = 18 | pages = 2314–29 |date=September 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 | title = Negative cross-talk between RelA and the glucocorticoid receptor: a possible mechanism for the antiinflammatory action of glucocorticoids | journal = Mol. Endocrinol. | volume = 9 | issue = 4 | pages = 401–12 |date=April 1995 | pmid = 7659084 | doi = 10.1210/me.9.4.401 }}</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 = J. Biol. Chem. | volume = 278 | issue = 43 | pages = 41779–88 |date=October 2003 | pmid = 12902338 | doi = 10.1074/jbc.M305350200 | citeseerx = 10.1.1.631.7318 | s2cid = 950035 }}</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 = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 21 | pages = 11776–81 |date=October 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 |url=https://archive.org/details/sim_molecular-and-cellular-biology_2000-03_20_6/page/2004 | journal = Mol. Cell. Biol. | volume = 20 | issue = 6 | pages = 2004–13 |date=March 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 Dev. | volume = 17 | issue = 20 | pages = 2564–77 |date=October 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 = J. Biol. Chem. | volume = 272 | issue = 49 | pages = 30607–10 |date=December 1997 | pmid = 9388192 | doi = 10.1074/jbc.272.49.30607 | doi-access = free }}</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 = 726–8 |date=October 1996 | pmid = 8878484 | doi = 10.1038/383726a0 | bibcode = 1996Natur.383..726S | s2cid = 4356272 }}</ref>
* [[Тиоредоксин]],<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 = J. Biol. Chem. | volume = 274 | issue = 5 | pages = 3182–8 |date=January 1999 | pmid = 9915858 | doi = 10.1074/jbc.274.5.3182 | doi-access = free }}</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 |url=https://archive.org/details/sim_molecular-and-cellular-biology_1998-10_18_10/page/5880 | journal = Mol. Cell. Biol. | volume = 18 | issue = 10 | pages = 5880–7 |date=October 1998 | pmid = 9742105 | pmc = 109174 | doi = 10.1128/mcb.18.10.5880}}</ref> и
* [[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 = J. Biol. Chem. | volume = 272 | issue = 13 | pages = 8153–6 |date=March 1997 | pmid = 9079630 | doi = 10.1074/jbc.272.13.8153 | doi-access = free }}</ref>.
{{Div col end}}

== Примечания ==
{{примечания}}

== Ссылки ==
* {{публикация|статья
|заглавие=Рецепторы глюкокортикоидов

|издание=База знаний по биологии человека
|ссылка=http://humbio.ru/humbio/endocrinology/0010f743.htm 
}}

{{Стероидные гормоны (экзогенные)}}

[[Категория:Белки человека]]
[[Категория:Факторы транскрипции]]