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Autor     Robert D. Ward, Nancy L. Weigel
Titel    Steroid Receptor Phosphorylation: Assigning Function to Site- Specific Phosphorylation
Zeitschrift    Biofactors
Ausgabe    35
Jahr    2009
Nummer    6
Seiten    528-536
DOI    10.1002/biof.66
URL    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2788675/pdf/nihms-153273.pdf

Literaturverz.   

no
Fußnoten    no
Fragmente    5


Fragmente der Quelle:
[1.] Rlm/Fragment 023 06 - Diskussion
Zuletzt bearbeitet: 2014-12-01 17:21:19 Singulus
Fragment, Gesichtet, Rlm, SMWFragment, Schutzlevel sysop, Verschleierung, Ward and Weigel 2009

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Like PR, the majority of identified phosphorylation sites for AR are located in the N-terminal domain. Although many of the NTD sites have been tested in vivo, assigning function to them has been difficult. Studies of transcriptional activation by AR on several androgen response elements containing promoters carried out in various cell lines has provided little information on the function of NTD sitespecific phosphorylation, Many phosphorylation mutants exhibited no aberrant activation characteristics when compared with wild type.(35,36,37,38). However, greater differences in activity can be detected when specific signaling pathways are activated or inhibited. For example, overexpression of cyclin D3/CDK11p58 inhibits AR activity by phosphorylating Ser308A mutant partially elevates hormone dependent activity and prevents cyclin D3/ CDK11p58- mediated repression of AR transcriptional activity (39).

35) Zhou, Z. X., Kemppainen, J. A., and Wilson, E. M. (1995) Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol. Endocrinol. 9, 605–615.

36) Zhu, Z., Becklin, R. R., Desiderio, D. M., and Dalton, J. T. (2001) Identification of a novel phosphorylation site in human androgen receptor by mass spectrometry. Biochem. Biophys. Res. Commun. 284, 836–844.

37) Yang, C. S., Vitto, M. J., Busby, S. A., Garcia, B. A., Kesler, C. T., Gioeli, D., Shabanowitz, J., Hunt, D. F., Rundell, K., Brautigan, D. L., and Paschal, B. M. (2005) Simian virus 40 small t antigen mediates conformation- dependent transfer of protein phosphatase 2A onto the androgen receptor. Mol. Cell Biol. 25, 1298–1308.

38) Gioeli, D., Ficarro, S. B., Kwiek, J. J., Aaronson, D., Hancock, M., Catling, A. D., White, F. M., Christian, R. E., Settlage, R. E., Shabanowitz, J., Hunt, D. F., and Weber, M. J. (2002) Androgen receptor phosphorylation. Regulation and identification of the phosphorylation sites. J. Biol. Chem. 277, 29304–29314.].

39) Zong, H., Chi, Y., Wang, Y., Yang, Y., Zhang, L., Chen, H., Jiang, J., Li, Z., Hong, Y., Wang, H., Yun, X., and Gu, J. (2007) Cyclin D3/CDK11p58 complex is involved in the repression of androgen receptor. Mol. Cell Biol. 27, 7125–7142.

Like PR, the majority of identified phosphorylation sites for AR are located in the N-terminal domain (Figure 2). Although many of the NTD sites have been verified in vivo, assigning function to them has been difficult. Studies of transcriptional activation by AR of several androgen response elements containing promoters carried out in various cell lines has provided little information as to the function of NTD site-specific phosphorylation as many phosphorylation mutants have exhibited no aberrant activation characteristics when compared to wild type (56-60). However, greater differences in activity can be detected when specific signaling pathways are activated or inhibited. For example, overexpression of cyclin D3/CDK11p58 inhibits AR activity. The kinase phosphorylates Ser308; substitution of an alanine elevates hormone dependent activity modestly and prevents cyclin D3/ CDK11p58 mediated repression of AR transcriptional activity (61).

56. Zhou ZX, Kemppainen JA, Wilson EM. Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol Endocrinol. 1995; 9:605–615. [PubMed: 7565807]

57. Zhu Z, Becklin RR, Desiderio DM, Dalton JT. Identification of a novel phosphorylation site in human androgen receptor by mass spectrometry. Biochem Biophys Res Commun. 2001; 284:836– 844. [PubMed: 11396978]

58. Yang CS, Vitto MJ, Busby SA, Garcia BA, Kesler CT, Gioeli D, Shabanowitz J, Hunt DF, Rundell K, Brautigan DL, Paschal BM. Simian virus 40 small t antigen mediates conformation dependent transfer of protein phosphatase 2A onto the androgen receptor. Mol Cell Biol. 2005; 25:1298–1308. [PubMed: 15684382]

59. Gioeli D, Ficarro SB, Kwiek JJ, Aaronson D, Hancock M, Catling AD, White FM, Christian RE, Settlage RE, Shabanowitz J, Hunt DF, Weber MJ. Androgen receptor phosphorylation. Regulation and identification of the phosphorylation sites. J Biol Chem. 2002; 277:29304–29314. [PubMed: 12015328]

60. Chen S, Xu Y, Yuan X, Bubley GJ, Balk SP. Androgen receptor phosphorylation and stabilization in prostate cancer by cyclin-dependent kinase 1. Proc Natl Acad Sci U S A. 2006; 103:15969–15974. [PubMed: 17043241]

61. Zong H, Chi Y, Wang Y, Yang Y, Zhang L, Chen H, Jiang J, Li Z, Hong Y, Wang H, Yun X, Gu J. Cyclin D3/CDK11p58 complex is involved in the repression of androgen receptor. Mol Cell Biol. 2007; 27:7125–7142. [PubMed: 17698582]

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[2.] Rlm/Fragment 024 01 - Diskussion
Zuletzt bearbeitet: 2014-12-01 17:22:47 Singulus
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Several studies have suggested that AKT-mediated phosphorylation of Ser213 and Ser791 (numbered based on an AR length of 919 amino acids) reduces AR activity (40). Mutation of the AR Ser213 to alanine caused resistance to AKT-mediated suppression of activity in DU145 cells(41) . Palazzolo et al. found that substituting alanines for both of the sites also prevented AKT-mediated inhibition of AR transcriptional activity. Surprisingly, substitution of aspartic acids at either site blocked hormone binding and, therefore, ligand-dependent AR protein stabilization, ligand-mediated translocation, and AR transcriptional activity(42).

The remaining sites in the AR NTD domain also have been shown to have important functional roles. When a fragment of the androgen receptor (amino acids 507-660) is expressed, Ser515 and Ser578 are phosphorylated in response to EGF treatment(43).

The AR Ser515Ala mutation exhibited a more severe phenotype than the Ser578Ala and the double mutant displayed little to no activity; furthermore, EGF treatment had no effect on the activity of this mutant.


40) Wen, Y., Hu, M. C., Makino, K., Spohn, B., Bartholomeusz, G., Yan, D. H., and Hung, M. C. (2000) HER-2/neu promotes androgenindependent survival and growth of prostate cancer cells through the Akt pathway. Cancer Res. 60, 6841–6845..

41) Taneja, S. S., Ha, S., Swenson, N. K., Huang, H. Y., Lee, P., Melamed, J., Shapiro, E., Garabedian, M. J., and Logan, S. K. (2005) Cell-specific regulation of androgen receptor phosphorylation in vivo. J. Biol. Chem. 280, 40916–40924..

42) Palazzolo, I., Burnett, B. G., Young, J. E., Brenne, P. L., La Spada, A. R., Fischbeck, K. H., Howell, B. W., and Pennuto, M. (2007) Akt blocks ligand binding and protects against expanded polyglutamine androgen receptor toxicity. Hum. Mol. Genet. 16, 1593–1603.

43) Ponguta, L. A., Gregory, C. W., French, F. S., and Wilson, E. M. (2008) Site-specific androgen receptor serine phosphorylation linked to epidermal growth factor-dependent growth of castration-recurrent prostate cancer. J. Biol. Chem. 283, 20989–21001.

Several studies have suggested that AKT mediated phosphorylation of Ser213 and Ser791 (numbered based on an AR length of 919 amino acids) reduces AR activity. Both sites are phosphorylated by the P13K/Akt signaling pathways (62-64). Mutation of the AR Ser213 to alanine caused AR to be resistant to AKT mediated suppression of activity in DU145 cells (64,65). Palazzolo et al found that substituting alanines for both of the sites also prevented

[page 7]

AKT mediated inhibition of AR transcriptional activity. Surprisingly, substitution of aspartic acids at either site blocked hormone binding and, therefore, ligand dependent AR protein stabilization, ligand-mediated translocation, and AR transcriptional activity (66).

The remaining sites in the AR NTD also have been shown to have important functional roles. When a fragment of the androgen receptor (amino acids 507-660) is expressed, Ser515 and Ser578 are phosphorylated in response to EGF treatment (67). The AR Ser515Ala mutation exhibited a more severe phenotype than the Ser578Ala and the double mutant displayed little to no activity; furthermore, EGF treatment had no effect on the activity of this mutant.


62. Wen Y, Hu MC, Makino K, Spohn B, Bartholomeusz G, Yan DH, Hung MC. HER-2/neu promotes androgen-independent survival and growth of prostate cancer cells through the Akt pathway. Cancer Res. 2000; 60:6841–6845. [PubMed: 11156376]

63. Taneja SS, Ha S, Swenson NK, Huang HY, Lee P, Melamed J, Shapiro E, Garabedian MJ, Logan SK. Cell-specific regulation of androgen receptor phosphorylation in vivo. J Biol Chem. 2005; 280:40916–40924. [PubMed: 16210317]

64. Lin HK, Yeh S, Kang HY, Chang C. Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor. Proc Natl Acad Sci U S A. 2001; 98:7200– 7205. [PubMed: 11404460]

65. Lin HK, Hu YC, Yang L, Altuwaijri S, Chen YT, Kang HY, Chang C. Suppression versus induction of androgen receptor functions by the phosphatidylinositol 3-kinase/Akt pathway in prostate cancer LNCaP cells with different passage numbers. J Biol Chem. 2003; 278:50902– 50907. [PubMed: 14555644]

66. Palazzolo I, Burnett BG, Young JE, Brenne PL, La Spada AR, Fischbeck KH, Howell BW, Pennuto M. Akt blocks ligand binding and protects against expanded polyglutamine androgen receptor toxicity. Hum Mol Genet. 2007; 16:1593–1603. [PubMed: 17470458]

67. Ponguta LA, Gregory CW, French FS, Wilson EM. Site-specific androgen receptor serine phosphorylation linked to epidermal growth factor-dependent growth of castration-recurrent prostate cancer. J Biol Chem. 2008; 283:20989–21001. [PubMed: 18511414]

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[3.] Rlm/Fragment 025 01 - Diskussion
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A Ser578Ala substitution results in increased nuclear localization of AR in the absence of ligand but eliminates AR transcriptional response to EGF. AR Ser578Ala also exhibits increased binding to Ku-70/80 regulatory subunits of DNA dependent protein kinase in addition to nuclear retention of the AR in association with hyperphosphorylation at Ser 515(44).

Finally, the Ser515Ala mutant is not phosphorylated on Ser650, which is located in the hinge region of AR (45).

One possible explanation for this effect is that phosphorylation at Ser515 mediates a conformational change of the AR thus making the Ser650 phosphosite either more available to phosphatases or less accessible to kinases. Attempting to assign function to the AR Ser650 phosphorylation site itself has produced conflicting reports. Early studies have suggested that blocking phosphorylation of this site resulted in 30% reduced activity with an MMTV-Luc reporter in CV1 cells . This was in direct contrast to later reports examining the function of Ser650 phosphorylation on AR activity in various cell lines using various reporters in which no phenotype was detected .


43) Ponguta, L. A., Gregory, C. W., French, F. S., and Wilson, E. M. (2008) Site-specific androgen receptor serine phosphorylation linked to epidermal growth factor-dependent growth of castration-recurrent prostate cancer. J. Biol. Chem. 283, 20989–21001.

44) Pierre Chymkowitch, Nicolas Le May, Pierre Charneau, Emmanuel Compe and Jean-Marc Egly. The phosphorylation of the androgen receptor by TFIIH directs the ubiquitin/proteasome process. EMBO J. 2011 Feb 2;30(3):468-79. Epub 2010 Dec 14

45) Wong, H. Y., Burghoorn, J. A., Van Leeuwen, M., De Ruiter, P. E., Schippers, E., Blok, L. J., Li, K. W., Dekker, H. L., De Jong, L., Trapman, J., Grootegoed, J. A., and Brinkmann, A. O. (2004) Phosphorylation of androgen receptor isoforms. Biochem. J. 383, 267–276.

A Ser578Ala substitution results in increased nuclear localization of AR in the absence of ligand but eliminates AR transcriptional response to EGF. AR Ser578Ala also exhibits increased binding to Ku-70/80 regulatory subunits of DNA-dependent protein kinase in addition to nuclear retention of the AR in association with hyperphosphorylation at Ser515 (67). Finally, the Ser515Ala mutant is not phosphorylated on Ser650, which is located in the hinge region of AR (68). One possible explanation for this is that phosphorylation at Ser515 mediates a conformational change of the AR thus making the Ser650 phospho site either more available to phosphatases or less accessible to kinases. Attempting to assign function to the AR Ser650 phosphorylation site itself has produced conflicting reports. Early studies have suggested that blocking phosphorylation of this site resulted in 30% reduced activity with an MMTV-Luc reporter in CV1 cells (56). This was in direct contrast to later reports examining the function of Ser650 phosphorylation on AR activity in various cell lines using various reporters in which no phenotype was detected (59,68).

56. Zhou ZX, Kemppainen JA, Wilson EM. Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol Endocrinol. 1995; 9:605–615. [PubMed: 7565807]

59. Gioeli D, Ficarro SB, Kwiek JJ, Aaronson D, Hancock M, Catling AD, White FM, Christian RE, Settlage RE, Shabanowitz J, Hunt DF, Weber MJ. Androgen receptor phosphorylation. Regulation and identification of the phosphorylation sites. J Biol Chem. 2002; 277:29304–29314. [PubMed: 12015328]

67. Ponguta LA, Gregory CW, French FS, Wilson EM. Site-specific androgen receptor serine phosphorylation linked to epidermal growth factor-dependent growth of castration recurrent prostate cancer. J Biol Chem. 2008; 283:20989–21001. [PubMed: 18511414]

68. Wong HY, Burghoorn JA, Van Leeuwen M, De Ruiter PE, Schippers E, Blok LJ, Li KW, Dekker HL, De Jong L, Trapman J, Grootegoed JA, Brinkmann AO. Phosphorylation of androgen receptor isoforms. Biochem J. 2004; 383:267–276. [PubMed: 15239671]

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[4.] Rlm/Fragment 026 01 - Diskussion
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However, careful examination of these studies revealed that the original observation by Zhuo et al. was evident at only high concentrations of receptor . Wong et al. also found that at high concentrations of receptor the Ser650Ala mutant is less active than wild type . AR Ser650 phosphorylation also plays an important role in nuclear export of AR in response to stress kinase signaling (29). A recent report has shown that protein phosphatase 1 (PP1) inhibition increases phosphorylation at AR Ser650 which causes a marked increase in nuclear export of AR which is not observed for the Ser650Ala mutant(46) .

This study suggests that PP1 plays a critical role in regulating AR protein stability and nuclear localization through dephosphorylation of AR at Ser650. In addition to Ser-Pro motifs, several tyrosine phosphorylation sites are present in the NTD of AR. A number of candidate sites have been identified in AR isolated from cells overexpressing Src. Based on the overall level of tyrosine phosphorylation in AR, substituting Phe for Tyr534 reduced the Tyr phosphorylation most substantially suggesting that this is a major site under these conditions(47).


29)Daniel Gioeli, Ben E. Black, Vicki Gordon, Adam Spencer, Cristina T. Kesler, Scott T. Eblen, Bryce M. Paschal, and Michael J. Weber. Stress Kinase Signaling Regulates Androgen Receptor Phosphorylation, Transcription, and Localization Mol Endocrinol. 2006 Mar;20(3):503-15. Epub 2005 Nov 10

46) Chen, S., Kesler, C. T., Paschal, B. M., and Balk, S. P. (2009) Androgen receptor phosphorylation and activity are regulated by an association with protein phosphatase 1. J. Biol. Chem. 284, 25576–25584.

47) Guo, Z., Dai, B., Jiang, T., Xu, K., Xie, Y., Kim, O., Nesheiwat, I., Kong, X., Melamed, J., Handratta, V. D., Njar, V. C., Brodie, A. M., Yu, L. R., Veenstra, T. D., Chen, H., and Qiu, Y. (2006) Regulation of androgen receptor activity by tyrosine phosphorylation. Cancer Cell. 10, 309–319.].

However, careful examination of these studies revealed that the original observation by Zhuo et al was evident at only high concentrations of receptor (56). Wong et al also found that at high concentrations of receptor the Ser650Ala mutant is less active than wild type (68). AR Ser650 phosphorylation also plays an important role in nuclear export of AR in response to stress kinase signaling (69). A recent report has shown that protein phosphatase 1 (PP1) inhibition increases phosphorylation at AR Ser650 which causes a marked increase in nuclear export of AR which is not observed for the Ser650Ala mutant (70). This study suggests that PP1 plays a critical role in regulating AR protein stability and nuclear localization through dephosphorylation of AR at Ser650.

In addition to Ser-Pro motifs, several tyrosine phosphorylation sites are present in the NTD of AR. A number of candidate sites have been identified in AR isolated from cells overexpressing Src. Based on the overall level of tyrosine phosphorylation in AR, substituting Phe for Tyr534 reduced the Tyr phosphorylation most substantially suggesting that this is a major site under these conditions (71).


56. Zhou ZX, Kemppainen JA, Wilson EM. Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol Endocrinol. 1995; 9:605–615. [PubMed: 7565807]

68. Wong HY, Burghoorn JA, Van Leeuwen M, De Ruiter PE, Schippers E, Blok LJ, Li KW, Dekker HL, De Jong L, Trapman J, Grootegoed JA, Brinkmann AO. Phosphorylation of androgen receptor isoforms. Biochem J. 2004; 383:267–276. [PubMed: 15239671]

69. Gioeli D, Black BE, Gordon V, Spencer A, Kesler CT, Eblen ST, Paschal BM, Weber MJ. Stress kinase signaling regulates androgen receptor phosphorylation, transcription, and localization. Mol Endocrinol. 2006; 20:503–515. [PubMed: 16282370]

70. Chen S, Kesler CT, Paschal BM, Balk SP. Androgen receptor phosphorylation and activity are regulated by an association with protein phosphatase 1. J Biol Chem. 2009

71. Guo Z, Dai B, Jiang T, Xu K, Xie Y, Kim O, Nesheiwat I, Kong X, Melamed J, Handratta VD, Njar VC, Brodie AM, Yu LR, Veenstra TD, Chen H, Qiu Y. Regulation of androgen receptor activity by tyrosine phosphorylation. Cancer Cell. 2006; 10:309–319. [PubMed: 17045208]

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[5.] Rlm/Fragment 027 01 - Diskussion
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The Tyr534Phe mutant also exhibited reduced activity and DNA binding at low doses of ligand and defective nuclear translocation in response to various stimuli . Finally, Tyr534Phe mutant expression caused growth inhibition in both cell lines and tumor xenografts containing the Tyr534Phe mutant grew more slowly than tumors expressing WT AR in castrated mice, thereby demonstrating a role for Tyr534 phosphorylation in prostate cancer cell growth under androgen-depleted conditions. Two additional tyrosine phosphorylation sites have been identified in cells treated with heregulin or transfected with constitutively active Ack (Cdc42 associated kinase).

Mutation of these sites, Tyr267 and Tyr363 to phenylalanine (Tyr267Phe and Tyr363Phe, respectively), reduced Ackinduced reporter activation and recruitment to the enhancer, thus demonstrating the importance of these sites in AR basal and liganddependent activity as well as in potentiation of AR activity by kinase signaling. In addition, substituting Phe at both of these sites also reduced tumor growth of Ack-driven tumor xenografts in castrated nude mice.

The Tyr534Phe mutant also exhibited reduced activity and DNA binding at low doses of ligand and defective nuclear translocation in response to various stimuli (71). Finally, Tyr534Phe mutant expression caused growth inhibition in both cell lines and tumor xenografts containing the Tyr534Phe mutant grew more slowly than tumors expressing WT AR in castrated mice, thereby demonstrating a role for Tyr534 phosphorylation in prostate cancer cell growth under androgen-depleted conditions (71). Two additional tyrosine phosphorylation sites have been identified in cells treated with heregulin or transfected with constitutively active Ack (Cdc42 associated kinase) (72). Mutation of these sites, Tyr267 and Tyr363 to phenylalanine (Tyr267Phe and Tyr363Phe, respectively), reduced Ack-induced reporter activation and recruitment to the enhancer, thus demonstrating the importance of these sites in AR basal and liganddependent activity as well as in potentiation of AR activity by kinase signaling (72). In addition, substituting Phe at both of these sites also reduced tumor growth of Ack-driven tumor xenografts in castrated nude mice (72).

71. Guo Z, Dai B, Jiang T, Xu K, Xie Y, Kim O, Nesheiwat I, Kong X, Melamed J, Handratta VD, Njar VC, Brodie AM, Yu LR, Veenstra TD, Chen H, Qiu Y. Regulation of androgen receptor activity by tyrosine phosphorylation. Cancer Cell. 2006; 10:309–319. [PubMed: 17045208]

72. Mahajan NP, Liu Y, Majumder S, Warren MR, Parker CE, Mohler JL, Earp HS, Whang YE. Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation. Proc Natl Acad Sci U S A. 2007; 104:8438–8443. [PubMed: 17494760]

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