Глюкокортикоидный рецептор: различия между версиями

Материал из Википедии — свободной энциклопедии
Перейти к навигации Перейти к поиску
Интерактивная навигация по истории
[отпатрулированная версия][непроверенная версия]
← Предыдущая правкаСледующая правка →
Содержимое удалено Содержимое добавлено
ВизуальныйВики-текст
м →‎Ссылки: ВП:Ф-О#электр. ресурс, removed: |тип=<nowiki>[электр. ресурс]</nowiki>
Нет описания правки
Строка 21: Строка 21:


[[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>.
[[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>.
==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 | 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 | 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 | 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 | 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 | 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 | 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 ==

Версия от 18:27, 3 августа 2021

Глюкокортикоидный рецептор
Обозначения
Символы NR3C1; GRL
Entrez Gene 2908
HGNC 7978
OMIM 138040
RefSeq NM_000176
UniProt P04150
Другие данные
Локус 5-я хр. , 5q31
Логотип Викиданных Информация в Викиданных ?

Глюкокортикоидный рецептор (англ. GR) — белок человека, рецептор глюкокортикоидов и фактор транскрипции, кодируемый геном GCCR на 5-й хромосоме. Относится к ядерным рецепторам, что отражено в названии (англ. nuclear receptor subfamily 3, group C, member 1, NR3C1).

Альтернативный сплайсинг порождает три изоформы рецептора: альфа, бета[1] и гамма[2].

Взаимодействия

Глюкокортикоидный рецептор взаимодействует с:


Примечания

  1. ↑ Oakley, R. H. The human glucocorticoid receptor beta isoform. Expression, biochemical properties, and putative function : [англ.] / R. H. Oakley, M. Sar, J. A. Cidlowski // Journal of Biological Chemistry. — 1996. — Vol. 271, no. 16 (April). — P. 9550—9559. — doi:10.1074/jbc.271.16.9550. — PMID 8621628.
  2. ↑ Rivers, C. Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing : [англ.] / C. Rivers, A. Levy, J. Hancock … [et al.] // Journal of Clinical Endocrinology and Metabolism[англ.]. — 1999. — Vol. 84, no. 11 (November). — P. 4283—4286. — doi:10.1210/jcem.84.11.6235. — PMID 10566686.
  3. ↑ Kullmann M, Schneikert J, Moll J, Heck S, Zeiner M, Gehring U, Cato AC (June 1998). "RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis". J. Biol. Chem. 273 (23): 14620—5. doi:10.1074/jbc.273.23.14620. PMID 9603979.
  4. ↑ Schneikert J, Hübner S, Langer G, Petri T, Jäättelä M, Reed J, Cato AC (December 2000). "Hsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptor". EMBO J. 19 (23): 6508—16. doi:10.1093/emboj/19.23.6508. PMC 305849. PMID 11101523.
  5. ↑ Boruk M, Savory JG, Haché RJ (November 1998). "AF-2-dependent potentiation of CCAAT enhancer binding protein beta-mediated transcriptional activation by glucocorticoid receptor". Mol. Endocrinol. 12 (11): 1749—63. doi:10.1210/mend.12.11.0191. PMID 9817600.
  6. ↑ Almlöf T, Wallberg AE, Gustafsson JA, Wright AP (June 1998). "Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau 1-core activation domain and target factors". Biochemistry. 37 (26): 9586—94. doi:10.1021/bi973029x. PMID 9649342.
  7. ↑ 1 2 Hulkko SM, Wakui H, Zilliacus J (August 2000). "The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function". Biochem. J. 349. Pt 3 (3): 885—93. doi:10.1042/bj3490885. PMC 1221218. PMID 10903152.
  8. ↑ Lin DY, Lai MZ, Ann DK, Shih HM (May 2003). "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". J. Biol. Chem. 278 (18): 15958—65. doi:10.1074/jbc.M300387200. PMID 12595526.
  9. ↑ Jibard N, Meng X, Leclerc P, Rajkowski K, Fortin D, Schweizer-Groyer G, Catelli MG, Baulieu EE, Cadepond F (March 1999). "Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR)". Exp. Cell Res. 247 (2): 461—74. doi:10.1006/excr.1998.4375. PMID 10066374.
  10. ↑ Kanelakis KC, Shewach DS, Pratt WB (September 2002). "Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly". J. Biol. Chem. 277 (37): 33698—703. doi:10.1074/jbc.M204164200. PMID 12093808.
  11. ↑ Hecht K, Carlstedt-Duke J, Stierna P, Gustafsson J, Brönnegârd M, Wikström AC (October 1997). "Evidence that the beta-isoform of the human glucocorticoid receptor does not act as a physiologically significant repressor". J. Biol. Chem. 272 (42): 26659—64. doi:10.1074/jbc.272.42.26659. PMID 9334248.
  12. ↑ de Castro M, Elliot S, Kino T, Bamberger C, Karl M, Webster E, Chrousos GP (September 1996). "The non-ligand binding beta-isoform of the human glucocorticoid receptor (hGR beta): tissue levels, mechanism of action, and potential physiologic role". Mol. Med. 2 (5): 597—607. doi:10.1007/BF03401643. PMC 2230188. PMID 8898375.
  13. ↑ van den Berg JD, Smets LA, van Rooij H (February 1996). "Agonist-free transformation of the glucocorticoid receptor in human B-lymphoma cells". J. Steroid Biochem. Mol. Biol. 57 (3—4): 239—49. doi:10.1016/0960-0760(95)00271-5. PMID 8645634. S2CID 20582144.
  14. ↑ Stancato LF, Silverstein AM, Gitler C, Groner B, Pratt WB (April 1996). "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". J. Biol. Chem. 271 (15): 8831—6. doi:10.1074/jbc.271.15.8831. PMID 8621522.
  15. ↑ Eggert M, Michel J, Schneider S, Bornfleth H, Baniahmad A, Fackelmayer FO, Schmidt S, Renkawitz R (November 1997). "The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U". J. Biol. Chem. 272 (45): 28471—8. doi:10.1074/jbc.272.45.28471. PMID 9353307.
  16. ↑ 1 2 3 4 5 Zilliacus J, Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson JA (April 2001). "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140". Mol. Endocrinol. 15 (4): 501—11. doi:10.1210/mend.15.4.0624. PMID 11266503.
  17. ↑ 1 2 Hittelman AB, Burakov D, Iñiguez-Lluhí JA, Freedman LP, Garabedian MJ (October 1999). "Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins". EMBO J. 18 (19): 5380—8. doi:10.1093/emboj/18.19.5380. PMC 1171607. PMID 10508170.
  18. ↑ Savory JG, Préfontaine GG, Lamprecht C, Liao M, Walther RF, Lefebvre YA, Haché RJ (February 2001). "Glucocorticoid receptor homodimers and glucocorticoid-mineralocorticoid receptor heterodimers form in the cytoplasm through alternative dimerization interfaces". Mol. Cell. Biol. 21 (3): 781—93. doi:10.1128/MCB.21.3.781-793.2001. PMC 86670. PMID 11154266.
  19. ↑ Tazawa H, Osman W, Shoji Y, Treuter E, Gustafsson JA, Zilliacus J (June 2003). "Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140". Mol. Cell. Biol. 23 (12): 4187—98. doi:10.1128/MCB.23.12.4187-4198.2003. PMC 156128. PMID 12773562.
  20. ↑ Subramaniam N, Treuter E, Okret S (June 1999). "Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids". J. Biol. Chem. 274 (25): 18121—7. doi:10.1074/jbc.274.25.18121. PMID 10364267.
  21. ↑ Stevens A, Garside H, Berry A, Waters C, White A, Ray D (May 2003). "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". Mol. Endocrinol. 17 (5): 845—59. doi:10.1210/me.2002-0320. PMID 12569182.
  22. ↑ Schulz M, Eggert M, Baniahmad A, Dostert A, Heinzel T, Renkawitz R (July 2002). "RU486-induced glucocorticoid receptor agonism is controlled by the receptor N terminus and by corepressor binding". J. Biol. Chem. 277 (29): 26238—43. doi:10.1074/jbc.M203268200. PMID 12011091.
  23. ↑ Kucera T, Waltner-Law M, Scott DK, Prasad R, Granner DK (July 2002). "A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1". J. Biol. Chem. 277 (29): 26098—102. doi:10.1074/jbc.M204013200. PMID 12118039.
  24. ↑ 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 (July 2002). "Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition". Cell. 110 (1): 93—105. doi:10.1016/S0092-8674(02)00817-6. PMID 12151000. S2CID 6955342.
  25. ↑ 1 2 3 Hsiao PW, Fryer CJ, Trotter KW, Wang W, Archer TK (September 2003). "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation". Mol. Cell. Biol. 23 (17): 6210—20. doi:10.1128/MCB.23.17.6210-6220.2003. PMC 180928. PMID 12917342.
  26. ↑ Préfontaine GG, Walther R, Giffin W, Lemieux ME, Pope L, Haché RJ (September 1999). "Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter". The Journal of Biological Chemistry. 274 (38): 26713—9. doi:10.1074/jbc.274.38.26713. PMID 10480874.
  27. ↑ Préfontaine GG, Lemieux ME, Giffin W, Schild-Poulter C, Pope L, LaCasse E, Walker P, Haché RJ (June 1998). "Recruitment of octamer transcription factors to DNA by glucocorticoid receptor". Molecular and Cellular Biology. 18 (6): 3416—30. doi:10.1128/MCB.18.6.3416. PMC 108923. PMID 9584182.
  28. ↑ 1 2 Rao MA, Cheng H, Quayle AN, Nishitani H, Nelson CC, Rennie PS (December 2002). "RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor". The Journal of Biological Chemistry. 277 (50): 48020—7. doi:10.1074/jbc.M209741200. PMID 12361945.
  29. ↑ Nissen RM, Yamamoto KR (September 2000). "The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain". Genes Dev. 14 (18): 2314—29. doi:10.1101/gad.827900. PMC 316928. PMID 10995388.
  30. ↑ Caldenhoven E, Liden J, Wissink S, Van de Stolpe A, Raaijmakers J, Koenderman L, Okret S, Gustafsson JA, Van der Saag PT (April 1995). "Negative cross-talk between RelA and the glucocorticoid receptor: a possible mechanism for the antiinflammatory action of glucocorticoids". Mol. Endocrinol. 9 (4): 401—12. doi:10.1210/me.9.4.401. PMID 7659084.
  31. ↑ Li G, Wang S, Gelehrter TD (October 2003). "Identification of glucocorticoid receptor domains involved in transrepression of transforming growth factor-beta action". J. Biol. Chem. 278 (43): 41779—88. CiteSeerX 10.1.1.631.7318. doi:10.1074/jbc.M305350200. PMID 12902338. S2CID 950035.{{cite journal}}: Википедия:Обслуживание CS1 (не помеченный открытым DOI) (ссылка)
  32. ↑ Song CZ, Tian X, Gelehrter TD (October 1999). "Glucocorticoid receptor inhibits transforming growth factor-beta signaling by directly targeting the transcriptional activation function of Smad3". Proc. Natl. Acad. Sci. U.S.A. 96 (21): 11776—81. Bibcode:1999PNAS...9611776S. doi:10.1073/pnas.96.21.11776. PMC 18362. PMID 10518526.
  33. ↑ Wallberg AE, Neely KE, Hassan AH, Gustafsson JA, Workman JL, Wright AP (March 2000). "Recruitment of the SWI-SNF chromatin remodeling complex as a mechanism of gene activation by the glucocorticoid receptor tau1 activation domain". Mol. Cell. Biol. 20 (6): 2004—13. doi:10.1128/MCB.20.6.2004-2013.2000. PMC 110817. PMID 10688647.
  34. ↑ Lerner L, Henriksen MA, Zhang X, Darnell JE (October 2003). "STAT3-dependent enhanceosome assembly and disassembly: synergy with GR for full transcriptional increase of the alpha 2-macroglobulin gene". Genes Dev. 17 (20): 2564—77. doi:10.1101/gad.1135003. PMC 218150. PMID 14522952.
  35. ↑ Zhang Z, Jones S, Hagood JS, Fuentes NL, Fuller GM (December 1997). "STAT3 acts as a co-activator of glucocorticoid receptor signaling". J. Biol. Chem. 272 (49): 30607—10. doi:10.1074/jbc.272.49.30607. PMID 9388192.
  36. ↑ Stöcklin E, Wissler M, Gouilleux F, Groner B (October 1996). "Functional interactions between Stat5 and the glucocorticoid receptor". Nature. 383 (6602): 726—8. Bibcode:1996Natur.383..726S. doi:10.1038/383726a0. PMID 8878484. S2CID 4356272.
  37. ↑ Makino Y, Yoshikawa N, Okamoto K, Hirota K, Yodoi J, Makino I, Tanaka H (January 1999). "Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function". J. Biol. Chem. 274 (5): 3182—8. doi:10.1074/jbc.274.5.3182. PMID 9915858.
  38. ↑ Chang CJ, Chen YL, Lee SC (October 1998). "Coactivator TIF1beta interacts with transcription factor C/EBPbeta and glucocorticoid receptor to induce alpha1-acid glycoprotein gene expression". Mol. Cell. Biol. 18 (10): 5880—7. doi:10.1128/mcb.18.10.5880. PMC 109174. PMID 9742105.
  39. ↑ Wakui H, Wright AP, Gustafsson J, Zilliacus J (March 1997). "Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein". J. Biol. Chem. 272 (13): 8153—6. doi:10.1074/jbc.272.13.8153. PMID 9079630.

Ссылки

Источник — https://ru.wikipedia.org/w/index.php?title=Глюкокортикоидный_рецептор&oldid=115854297