The Androgen Receptor Can Promote β-Catenin Nuclear Translocation Independently of Adenomatous Polyposis Coli

We provide evidence that the androgen receptor (AR) can promote nuclear translocation of β-catenin in LNCaP and PC3 prostate cancer cells. Using AR-expressing cells (LNCaP) and non-AR-expressing cells (PC3) we showed by time course cell fractionation that the AR can shuttle β-catenin into the nucleus when exposed to exogenous androgen. Cells exposed to the synthetic androgen, R1881, show distinct, punctate, nuclear co-localization of the AR and β-catenin. We further showed that the AR does not interact with adenomatous polyposis coli or glycogen synthase kinase-3β and, therefore, conclude that androgen-mediated transport of β-catenin occurs through a distinct pathway. The minimal necessary components of the AR and β-catenin required for binding nuclear accumulation of β-catenin nuclear import appears to be the DNA/ligand binding regions and the Armadillo repeats of β-catenin. We also employed a novel DNA binding assay to illustrate that β-catenin has the capacity to bind to the probasin promoter in an AR-dependent manner. The physiological relevance of AR-mediated transport of β-catenin and binding to an AR promoter appeared to be a substantial increase in AR transcriptional reporter activity. AR-mediated import represents a novel mode of nuclear accumulation of β-catenin. We provide evidence that the androgen receptor (AR) can promote nuclear translocation of β-catenin in LNCaP and PC3 prostate cancer cells. Using AR-expressing cells (LNCaP) and non-AR-expressing cells (PC3) we showed by time course cell fractionation that the AR can shuttle β-catenin into the nucleus when exposed to exogenous androgen. Cells exposed to the synthetic androgen, R1881, show distinct, punctate, nuclear co-localization of the AR and β-catenin. We further showed that the AR does not interact with adenomatous polyposis coli or glycogen synthase kinase-3β and, therefore, conclude that androgen-mediated transport of β-catenin occurs through a distinct pathway. The minimal necessary components of the AR and β-catenin required for binding nuclear accumulation of β-catenin nuclear import appears to be the DNA/ligand binding regions and the Armadillo repeats of β-catenin. We also employed a novel DNA binding assay to illustrate that β-catenin has the capacity to bind to the probasin promoter in an AR-dependent manner. The physiological relevance of AR-mediated transport of β-catenin and binding to an AR promoter appeared to be a substantial increase in AR transcriptional reporter activity. AR-mediated import represents a novel mode of nuclear accumulation of β-catenin. The androgen receptor (AR) 1The abbreviations used are: ARandrogen receptorGRglucocorticoid receptorERestrogen receptorRARretinoic acid receptorTRthyroid receptor, Nt, amino-terminal domainCtcarboxyl-terminal domainDBDDNA binding domainLBDligand binding domainAPCadenomatous polyposis coliGSK-3Bglycogen synthase kinase-3BTCFT cell factorGSTglutathione S-transferaseDHTdihydrotestosteroneLEFlymphoid enhancer factorAREandrogen response elementFBSfetal bovine serumWTwild-typeHAhemagglutininDAPI4′,6-diamidino-2-phenyl-indoleACDCacrydite capture of DNA complexNF-1nuclear factor-1NEnuclear extractCMVcytomegalovirusHspheat-shock proteinPB-acacrydite probasinMCS-acacrydite multiple cloning site has a fundamental role in development and differentiation of androgen-sensitive tissue but also has an important role in prostate cancer (1Quigley C.A., De Bellis A. Marschke K.B. el-Awady M.K. Wilson E.M. French F.S. Endocrine Rev. 1995; 16: 271-321Crossref PubMed Google Scholar). Proliferation of prostatic epithelium is dependent on the uptake of androgens from the serum through the cell membrane, binding to the cognate steroid receptors, and translocation to the nucleus leading to activation of transcription (2Rennie P.S. Bruchovsky N. Leco K.J. Sheppard P.C. McQueen S.A. Cheng H. Snoek S. Hamel A. Bock M.E. MacDonald B.S. Nickel B.E. Chang C. Liao S. Cattini P.A. Matusik R.J. Mol. Endocrinol. 1993; 7: 23-36Crossref PubMed Scopus (215) Google Scholar, 3Reid K.J. Hendy S.C. Saito J. Sorensen P. Nelson C.C. J. Biol. Chem. 2001; 276: 2943-2953Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar) of downstream genes (4Hager G.L. Lim C.S. Elbi C. Baumann C.T. J. Steroid Biochem. Mol Biol. 2000; 30: 249-254Crossref Scopus (112) Google Scholar). Structurally, the AR belongs to a superfamily of ligand-activated transcription factors composed of a highly conserved DNA binding domain (ARDBD) and a moderately conserved ligand binding domain (ARLBD), while containing an N-terminal domain (ARNt), which is least conserved (5Evans R.M. Science. 1988; 240: 889-895Crossref PubMed Scopus (6341) Google Scholar, 6Jenster G. van der Korput H.A. van Vroonhoven C. van der Kwast T.H. Trapman J. Brinkman A.O. Mol. Endocrinol. 1991; 5: 1396-1404Crossref PubMed Scopus (421) Google Scholar, 7MacLean H.E. Warne G.L. Zajac J.D. J. Steroid Biochem. Mol. Biol. 1997; 62: 233-242Crossref PubMed Scopus (120) Google Scholar). The ARNt contains a ligand-independent transcriptional activating function whereas the ARCt contains one that is ligand-dependent (8Snoek R. Bruchovsky N. Kasper S. Matusik R.J. Gleave M. Sato N. Mawji N.R. Rennie P.S. The Prostate. 1998; 36: 256-263Crossref PubMed Scopus (40) Google Scholar). The ligand binding domain of nuclear receptors interact with a variety of other proteins following ligand binding (9Danielian P.S. White R. Lees A. Parker M.G. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors..EMBO J. 1992; 11: 1025-1033Crossref PubMed Scopus (722) Google Scholar), which has the potential to augment or modulate transcriptional response. The transcriptional activity of the AR is largely determined by the presence or absence of other co-factors, including co-activators, which enhance AR activity, and co-repressors, which repress AR activity. Examples of previously identified co-activating molecules of the AR include CBP, SRC1, and TIF-2 (10Ikonen T. Palvimo J.J. Janne O.A. J. Biol. Chem. 1997; 272: 29821-29828Abstract Full Text Full Text PDF PubMed Scopus (311) Google Scholar, 11Yeh S. Chang H.C. Miyamoto H. Takatera H. Rahman M., Hy, K. Thin T.H. Lin H.K. Chang C. Keio J. Med. 1999; 2: 87-92Crossref Scopus (50) Google Scholar, 12Janne O.A. Moilanen A.M. Poukka H. Rouleau N. Karvonen U. Kotaja N. Hakli M. Palvimo J.J. Biochem. Soc. Trans. 2000; 4: 401-405Crossref Scopus (80) Google Scholar). androgen receptor glucocorticoid receptor estrogen receptor retinoic acid receptor thyroid receptor, Nt, amino-terminal domain carboxyl-terminal domain DNA binding domain ligand binding domain adenomatous polyposis coli glycogen synthase kinase-3B T cell factor glutathione S-transferase dihydrotestosterone lymphoid enhancer factor androgen response element fetal bovine serum wild-type hemagglutinin 4′,6-diamidino-2-phenyl-indole acrydite capture of DNA complex nuclear factor-1 nuclear extract cytomegalovirus heat-shock protein acrydite probasin acrydite multiple cloning site There is strong documentation to suggest steroid receptor shuttling upon exposure to the cognate ligand. Such studies have pertained to the AR (13Georget V. Lobaccaro J.M. Terouanne B. Mangeat P. Nicolas J.C. Sultan C. Mol. Cell Endocrinol. 1997; 129: 17-26Crossref PubMed Scopus (159) Google Scholar, 14Rakesh K.T. Lavrovsky Y. Ahn S.C. Song C.S. Chatterjee B. Roy A.K. Mol. Endocrinol. 2000; 14: 1162-1174Crossref PubMed Google Scholar, 15Tyagi R.K. Lavrosky Y. Soon C.A. Chung S.S. Chatterjee B. Roy K. Mol. Endocrinol. 2000; 8: 1162-1174Crossref Scopus (251) Google Scholar, 16Tomura A. Goto K. Morinaga H. Nomura M. Okabe T. Yanase T. Takayanagi R. Nawata H. J. Biol. Chem. 2001; 276: 28395-28401Abstract Full Text Full Text PDF PubMed Scopus (116) Google Scholar), glucocorticoid receptor (GR) (17Hache R.J.G. Tse R. Reich T. Savory J.G.A. Lefebvre Y.A. J. Biol. Chem. 1999; 274: 1432-1439Abstract Full Text Full Text PDF PubMed Scopus (99) Google Scholar), estrogen receptor (ER) (19Stenoien D.L. Mancini M.G. Patel K. Allegretto E.A. Smith C.L. Mancini M.A. Mol. Endocrinol. 2000; 14: 518-534PubMed Google Scholar), mineralocorticoid receptor (20Fejes-Toth G. Pearce D. Naray-Fejes-Toth A. Proc. Natl. Acad. Sci. U. S. A. 1998; 96: 2973-2978Crossref Scopus (214) Google Scholar), and thyroid receptor (TR) (21Zhu X.G. Hanover J.A. Hager G.L. Cheng S.Y. J. Biol. Chem. 1998; 42: 27058-27063Abstract Full Text Full Text PDF Scopus (100) Google Scholar). These receptors show a certain degree of trafficking either to or from the nucleus but also in a subnuclear fashion. Those that show a strong migration to the nucleus upon exposure to ligand are termed “translocating receptors” and can be contrasted with receptors that are constitutively nuclear (4Hager G.L. Lim C.S. Elbi C. Baumann C.T. J. Steroid Biochem. Mol Biol. 2000; 30: 249-254Crossref Scopus (112) Google Scholar). The ER shows expression that is mainly nuclear in the absence of ligand (22Htun H. Holth L.T. Walker D. Davie J.R. Hager G.L. Mol. Biol. Cell. 1999; 10: 471-486Crossref PubMed Scopus Google Scholar), whereas the AR and show a that is and nuclear H. S. K. K. Proc. Natl. Acad. Sci. U. S. A. 1995; PubMed Scopus Google Scholar, H. Holth L.T. Walker D. Davie J.R. Hager G.L. Mol. Biol. Cell. 1999; 10: 471-486Crossref PubMed Scopus Google Scholar). are to of AR in the J.A. M. French F.S. Wilson E.M. J. Biol. Chem. 1991; Full Text PDF Google Scholar) and in the nucleus G. van der Korput H.A. van Vroonhoven C. van der Kwast T.H. Trapman J. Brinkman A.O. Mol. Endocrinol. 1991; 5: 1396-1404Crossref PubMed Scopus (421) Google Scholar) in cell receptor by or of including R1881, the AR from heat-shock to the and (4Hager G.L. Lim C.S. Elbi C. Baumann C.T. J. Steroid Biochem. Mol Biol. 2000; 30: 249-254Crossref Scopus (112) Google Scholar). for steroid hormone receptor can be to the AR and the receptor is in the and upon ligand binding that translocation to the to of R.K. Lavrosky Y. Soon C.A. Chung S.S. Chatterjee B. Roy K. Mol. Endocrinol. 2000; 8: 1162-1174Crossref Scopus (251) Google Scholar). the nucleus of the receptor superfamily the nucleus in the presence of ligand (4Hager G.L. Lim C.S. Elbi C. Baumann C.T. J. Steroid Biochem. Mol Biol. 2000; 30: 249-254Crossref Scopus (112) Google Scholar). that are or with steroid receptors into the nucleus have not with the of the AR to to the we that the AR other molecules to the Examples of are to nuclear and subnuclear trafficking for of and AR transcriptional activation R.K. Lavrosky Y. Soon C.A. Chung S.S. Chatterjee B. Roy K. Mol. Endocrinol. 2000; 8: 1162-1174Crossref Scopus (251) Google Scholar). the ligand-dependent the AR and β-catenin S. 2000; Scholar), we that β-catenin be of a complex that to the nucleus a to nuclear is a a role in cell by with and the to N. H. 2000; 11: Scopus Google Scholar, P. Cell. 2001; 5: Full Text Full Text PDF Scopus Google Scholar). to role β-catenin is a in the pathway. is important in tissue development and differentiation A. R. Rev. Cell. Biol. 1998; 14: PubMed Scopus Google Scholar) in P. Cell. 2001; 5: Full Text Full Text PDF Scopus Google Scholar). the absence of β-catenin is mainly cell but also with including adenomatous polyposis coli Mol. 2001; 7: Scopus Google glycogen synthase kinase-3β R. B. P. Biol. 1998; 10: Full Text Full Text PDF Google Scholar), and R. B. P. Biol. 1998; 10: Full Text Full Text PDF Google Scholar). β-catenin is by and for by the complex R. B. P. Biol. 1998; 10: Full Text Full Text PDF Google Scholar). of the and for accumulation of β-catenin in the β-catenin can to the with and interact with the to expression of cell of the that are to be by a include and A. R. J. 2000; Scopus Google Scholar). of is the in which β-catenin is to the β-catenin does not have a nuclear Cell Biol. 2000; 2: PubMed Scopus Google Scholar), polyposis can a shuttling protein Cell Biol. 2000; 2: PubMed Scopus Google Scholar). Such studies have that of the nuclear on nuclear β-catenin and that can shuttle the nucleus and while β-catenin to important also contains nuclear that are necessary for nuclear activity White Proc. Natl. Acad. Sci. U. S. A. 2000; Scopus Google Scholar) and for studies have that nuclear of β-catenin can of the protein and that be with β-catenin transport A. M. B. J. Biol. Chem. 2001; 276: Full Text Full Text PDF PubMed Scopus Google Scholar). studies have also that β-catenin can to the nucleus of the shuttling protein N. T. Y. Mol. Biol. Cell. 1999; 10: PubMed Scopus Google Scholar). is the of the identified ligand-dependent β-catenin and the we used and a novel DNA binding assay to provide evidence that β-catenin in an AR ligand-dependent the to an we the of the AR and β-catenin to protein and to transcriptional we that AR can β-catenin to the nucleus in an AR ligand-dependent a distinct that is of we identified the components of the AR and β-catenin that are necessary and for PC3 and cells in containing and LNCaP cells in containing Cells in for with the following expression β-catenin β-catenin β-catenin repeats β-catenin AR AR AR AR AR and Cells with steroid receptor ligand in AR cells by of AR and expression previously (8Snoek R. Bruchovsky N. Kasper S. Matusik R.J. Gleave M. Sato N. Mawji N.R. Rennie P.S. The Prostate. 1998; 36: 256-263Crossref PubMed Scopus (40) Google β-catenin from and of receptor expression from Cells in in on in for and Cells in serum in for β-catenin and AR binding used a of and for by to used a and for by with containing on used a and of to and a least in and cells with ligand for to to cells in and into and nuclear the and for protein the protein assay cell with with a and with on for with the of a Cell for for and by with to of the of of to in containing in by and the proteins a with in in for and for with either β-catenin N-terminal DNA binding domain or domain with either or and and in the used of of or of of DNA to a of with for and either used for binding or The of in by by and following in with and exposed to proteins with in a of with binding and and with for with of binding in and by and exposed to The assay and J. in Scholar) by androgen receptor DNA binding domain DNA or with acrydite binding or acrydite binding The nuclear factor-1 acrydite a binding in the of a acrydite on a and with LNCaP nuclear with with and the of a the protein from the acrydite by and with an DNA or with acrydite probasin promoter to or the acrydite multiple cloning site by with a PC3 and LNCaP cells in and Cells with a of of DNA for to the cells in serum containing R1881, or for least in least and the The of AR and β-catenin with to the DNA binding domain of the AR and of β-catenin in LNCaP cells that with and for by and in suggest that in the absence of androgen the AR the whereas β-catenin cell in the and the the presence of ligand we a of AR which also showed nuclear in cells upon ligand and in with AR whereas in not of β-catenin cell not to in response to AR whereas appeared to and a to the trafficking of the we determined the of binding the AR and β-catenin. we used AR including and and in from expression the or and of the AR the strong the β-catenin repeats and AR The repeats showed with the but with the a role for the and in binding AR and β-catenin. the in we to a binding in the presence or absence of ligand. We have to potential of by proteins in the cell in absence of which is not in the transcriptional and shuttling time β-catenin to to the nucleus in an we a of cell on LNCaP cells and AR cells a time course of androgen exposure and nuclear determined by nuclear for and for The of in nuclear and in the an of We further protein through a time course by and nuclear LNCaP cells that with and into and nuclear and showed a accumulation of nuclear β-catenin We a increase in nuclear of nuclear accumulation of AR and β-catenin suggest a of in β-catenin when with in nuclear β-catenin is for by the of β-catenin that that that does not upon of AR ligand. the in β-catenin in and nuclear in LNCaP which with expression for β-catenin by LNCaP cells with either and β-catenin we a of nuclear accumulation of the β-catenin with cells. showed a in nuclear accumulation of β-catenin and a a of nuclear We further to AR-dependent of β-catenin other AR including the physiological androgen, R1881, nuclear accumulation of the AR and β-catenin to a with not We other cancer cell including cells AR-mediated β-catenin nuclear we cell and and and β-catenin We a of nuclear accumulation of β-catenin to that in LNCaP β-catenin from the not the of the We further the of nuclear and β-catenin in cells by of AR the absence of androgen, AR in the by and whereas in the nuclear of cells with ligand. We β-catenin with AR and in the absence of androgen the presence of a with LNCaP We further that of the complex in androgen but in presence evidence that the AR can β-catenin to the nucleus in LNCaP and we to other nuclear receptors have in PC3 prostate cancer cells. we used a prostate cancer cell that not the androgen PC3 cells with ER or β-catenin we an to β-catenin to the nucleus with ligand the shows an to to the nucleus upon exposure to with β-catenin not in cell in β-catenin translocation with the AR we to β-catenin AR PC3 cells the expression and that of the of the AR showed to β-catenin to the nucleus the a expression but not show ligand-dependent in nuclear of or β-catenin a function of ligand cells with the the ligand-dependent translocation of β-catenin to the of the DNA binding domain and the ligand binding domain of the AR for β-catenin nuclear a the AR and β-catenin. accumulation in PC3 cells to that in in that appeared to We further that the repeats are necessary and for AR-dependent nuclear translocation of the and components of showed whereas the repeats showed accumulation to the nucleus AR-mediated import of β-catenin a distinct we the AR the to interact with and in cell with and we AR for AR and β-catenin We in AR a function of hormone but a ligand AR and which is with AR in the presence of androgen. showed a distinct but not in AR showed and These also not AR either with or ligand. on the that protein to a DNA a binding exposed to a Such and by showed that the androgen receptor from nuclear receptor with to by the presence of the of the in the from the binding AR also with androgen response and with a of binding with including a binding for and binding DNA the of of the androgen receptor in nuclear extract binding and by the with the DNA binding region of the AR with that which is to the DNA when binding for β-catenin a promoter to of β-catenin of β-catenin in binding including the multiple cloning or binding These the presence of a ligand-dependent complex with the probasin LNCaP nuclear with and the nuclear components by show a of AR and β-catenin in the presence of ligand that are into the nuclear to a in the presence of ligand. Using PC3 cells we to the components of the AR and β-catenin that necessary for ligand-dependent transcriptional we AR and β-catenin into PC3 cells and activity a function of β-catenin. We that AR containing transcriptional response whereas AR the the showed activation and by β-catenin. Cells with the and the showed a and ligand-dependent transcriptional response to β-catenin the of the for ligand-dependent of the AR by β-catenin for AR-mediated translocation of β-catenin. Cells with the ARNt or showed transcriptional activity. for the repeats to enhance the AR transcriptional response the reporter in a ligand-dependent but not to the the β-catenin. of the the of β-catenin to augment AR transcription receptor trafficking of β-catenin is a for β-catenin does not have an identified nuclear dependent upon other molecules for nuclear the nuclear the AR and β-catenin are ligand AR-mediated transport of β-catenin appears to be distinct from transport of β-catenin. transcriptional activity of AR is with of β-catenin when in the presence of ligand. we evidence for a novel and distinct by which β-catenin can the nucleus of AR cancer cell We showed that upon exposure to androgen the AR is of shuttling β-catenin to the a by which β-catenin can augment the transcriptional activity of AR mode of import appears to be of the β-catenin studies suggest co-localization of AR and β-catenin in the nucleus of LNCaP prostate cancer cells in the presence of studies suggest a but not with or evidence for an complex that can bind to an promoter a novel DNA binding we evidence that the β-catenin Armadillo and the is for ligand-dependent nuclear translocation and transcriptional Using we showed that β-catenin can with AR for the DNA binding region of the receptor in the presence of androgen. The of other steroid receptors in the nucleus has and, with the (17Hache R.J.G. Tse R. Reich T. Savory J.G.A. Lefebvre Y.A. J. Biol. Chem. 1999; 274: 1432-1439Abstract Full Text Full Text PDF PubMed Scopus (99) Google Scholar), ER H. J. D.L. Hager G.L. Proc. Natl. Acad. Sci. U. S. A. PubMed Scopus Google Scholar), and J.A. B.S. J. Mol. Endocrinol. 2001; 4: Scholar), the AR shows a distinct upon exposure to ligand. the and not show substantial migration to the nucleus upon of is to that is subnuclear trafficking of of nuclear proteins in cells of protein with the and other co-factors, including CBP, and These studies are The co-localization of the AR and β-catenin not by that are AR by β-catenin and, β-catenin that are by the The co-localization of β-catenin with the AR also that β-catenin be with the transcriptional of LNCaP cells. with the of a novel DNA binding Using an acrydite we to show AR-dependent binding of β-catenin to the probasin that β-catenin have the capacity to modulate the cell in prostate cancer cells in an by of downstream transcription factors B. S. R. M. 2001; PubMed Scopus Google Scholar) and the M. C. C. Janne O.A. Palvimo J.J. Mol. Endocrinol. 2001; PubMed Scopus Google Scholar). is that β-catenin downstream transcription factors by an AR in a manner. the AR have an on the other steroid receptors the and have to repress the pathway. Such a ligand-dependent suggest of nuclear β-catenin promoter AR-mediated translocation of β-catenin with and with the of AR the nucleus by the of ligand. time not not of AR or β-catenin AR cells (LNCaP) and AR-expressing cells time cell showed a nuclear translocation of β-catenin. The of β-catenin in in the We to the that the of β-catenin with the AR and to to the nucleus is with the of β-catenin. is that the of β-catenin cell The of of β-catenin has in studies and be important in AR Nelson J. Biol. Chem. 1997; 272: Full Text Full Text PDF PubMed Scopus Google Scholar) have identified distinct of which are of a and AR β-catenin. be to other are a function of the of β-catenin upon nuclear to an of be to the and transcription is the of nuclear of β-catenin of which are in a of nuclear receptors and β-catenin. showed of ER the and the that the ER is in the nucleus with or the presence of ligand (22Htun H. Holth L.T. Walker D. Davie J.R. Hager G.L. Mol. Biol. Cell. 1999; 10: 471-486Crossref PubMed Scopus Google Scholar). that we not nuclear translocation of and the to β-catenin transcriptional activity K. A. R. G. 2001; PubMed Scopus Google Scholar, V. M. S. Biol. 1999; Full Text Full Text PDF Google Scholar) we not to trafficking of β-catenin with receptors, we the that the and of receptors β-catenin is to the Such a of trafficking not be with the used in The that does not β-catenin translocation in the AR does be a function of the cell used in the that cells that of show a to β-catenin with prostate cancer cell studies cell a and β-catenin. We to the required components for translocation of β-catenin to the a of into PC3 cells we to that β-catenin the region for binding but the for ligand-dependent nuclear These are with the of the ligand binding domain for nuclear showed a degree of nuclear in cells that but not in ligand-dependent when cells with protein we determined that the region is of a strong the that of not by be into the nucleus by the of the we the the AR and β-catenin a function of the presence of ligand we not to the absence of proteins that We further the minimal of AR and β-catenin for nuclear translocation and that ligand-dependent be and the repeats of β-catenin. The repeats of β-catenin are binding for other including CBP, and The of the region of binding to a region the DNA binding domain of steroid receptors is LNCaP and PC3 prostate cancer cells are in to the of AR-mediated nuclear translocation of β-catenin. is mainly to constitutively activity of and highly K. B. G. D. M. 2000; Google Scholar), a of and can be to the with which cell the of β-catenin are other cell activity are that β-catenin have the potential for other binding steroid β-catenin we to the of exogenous β-catenin. for the β-catenin showed a translocation of the of by previously AR-dependent of β-catenin appears to be of the of β-catenin from the to the nucleus and to the in cancer cells that can be but can also from of β-catenin. of AR transport of β-catenin shows that upon ligand heat-shock proteins also from the AR for of β-catenin also the AR nuclear which promote translocation of an complex into the nucleus and binding to one or AR of an AR-mediated trafficking to the for a role in of the promote β-catenin and AR transcriptional activity. nuclear β-catenin in cell or studies include of the AR and other nuclear receptors interact with the pathway. the degree of the DNA binding regions the nuclear receptor is that are the and ER with to genes a function of ligand the of β-catenin to augment transcriptional activity of other nuclear receptors is a and to further studies in the and the in β-catenin interact with the nuclear receptors, is are to β-catenin receptor to studies of steroid receptor transcriptional to the with nuclear receptors in the nuclear receptor and but also and with the potential to

Récupéré en direct depuis OpenAlex et désinversé. Les résumés ne sont pas conservés dans cette base de données : les index inversés représentent 8,6 Go des 9,3 Go de texte de la base, et le serveur dispose de 13 Go libres.