메뉴 건너뛰기




Volumn 319, Issue 1, 2004, Pages 275-282

The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway

Author keywords

BMP; PIASy; RING domain; Smad; Transcription

Indexed keywords

BONE MORPHOGENETIC PROTEIN 2; PROTEIN INHIBITOR; PROTEIN PIASY; SMAD PROTEIN; STAT PROTEIN; UNCLASSIFIED DRUG;

EID: 2442686416     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.04.161     Document Type: Article
Times cited : (11)

References (48)
  • 1
    • 0031105160 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: An unconventional approach to isolation of first mammalian morphogens
    • Reddi A.H. Bone morphogenetic proteins: an unconventional approach to isolation of first mammalian morphogens. Cytokine Growth Factor Rev. 8:1997;11-20
    • (1997) Cytokine Growth Factor Rev. , vol.8 , pp. 11-20
    • Reddi, A.H.1
  • 2
    • 0029737070 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: Multifunctional regulators of vertebrate development
    • Hogan B.L. Bone morphogenetic proteins: multifunctional regulators of vertebrate development. Genes Dev. 10:1996;1580-1594
    • (1996) Genes Dev. , vol.10 , pp. 1580-1594
    • Hogan, B.L.1
  • 4
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massagué J. TGF-β signal transduction. Annu. Rev. Biochem. 67:1998;753-791
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massagué, J.1
  • 5
    • 0031438047 scopus 로고    scopus 로고
    • TGF-β signalling from cell membrane to nucleus through SMAD proteins
    • Heldin C.H., Miyazono K., ten Dijke P. TGF-β signalling from cell membrane to nucleus through SMAD proteins. Nature. 390:1997;465-471
    • (1997) Nature , vol.390 , pp. 465-471
    • Heldin, C.H.1    Miyazono, K.2    Ten Dijke, P.3
  • 6
    • 0032442852 scopus 로고    scopus 로고
    • Smads: Transcriptional activators of TGF-β responses
    • Derynck R., Zhang Y., Feng X.H. Smads: transcriptional activators of TGF-β responses. Cell. 95:1998;737-740
    • (1998) Cell , vol.95 , pp. 737-740
    • Derynck, R.1    Zhang, Y.2    Feng, X.H.3
  • 7
    • 0031723689 scopus 로고    scopus 로고
    • Bone morphogenetic protein 6 in skeletal metastases from prostate cancer and other common human malignancies
    • Autzen P., Robson C.N., Bjartell A., Malcolm A.J., Johnson M.I., Neal D.E., Hamdy F.C. Bone morphogenetic protein 6 in skeletal metastases from prostate cancer and other common human malignancies. Br. J. Cancer. 78:1998;1219-1223
    • (1998) Br. J. Cancer , vol.78 , pp. 1219-1223
    • Autzen, P.1    Robson, C.N.2    Bjartell, A.3    Malcolm, A.J.4    Johnson, M.I.5    Neal, D.E.6    Hamdy, F.C.7
  • 8
    • 0342657717 scopus 로고    scopus 로고
    • Expression of bone morphogenetic protein receptors type-IA, -IB and -II correlates with tumor grade in human prostate cancer tissues
    • Kim I.Y., Lee D.H., Ahn H.J., Tokunaga H., Song W., Devereaux L.M., Jin D., Sampath T.K., Morton R.A. Expression of bone morphogenetic protein receptors type-IA, -IB and -II correlates with tumor grade in human prostate cancer tissues. Cancer Res. 60:2000;2840-2844
    • (2000) Cancer Res. , vol.60 , pp. 2840-2844
    • Kim, I.Y.1    Lee, D.H.2    Ahn, H.J.3    Tokunaga, H.4    Song, W.5    Devereaux, L.M.6    Jin, D.7    Sampath, T.K.8    Morton, R.A.9
  • 9
    • 0033571408 scopus 로고    scopus 로고
    • Bone morphogenetic protein-6 is a marker of serous acinar cell differentiation in normal and neoplastic human salivary gland
    • Heikinheimo K.A., Laine M.A., Ritvos O.V., Voutilainen R.J., Hogan B.L., Leivo I.V., Heikinheimo A.K. Bone morphogenetic protein-6 is a marker of serous acinar cell differentiation in normal and neoplastic human salivary gland. Cancer Res. 59:1999;5815-5821
    • (1999) Cancer Res. , vol.59 , pp. 5815-5821
    • Heikinheimo, K.A.1    Laine, M.A.2    Ritvos, O.V.3    Voutilainen, R.J.4    Hogan, B.L.5    Leivo, I.V.6    Heikinheimo, A.K.7
  • 11
    • 0041314104 scopus 로고    scopus 로고
    • Identification of a putative autocrine bone morphogenetic protein-signaling pathway in human ovarian surface epithelium and ovarian cancer cells
    • Shepherd T.G., Nachtigal M.W. Identification of a putative autocrine bone morphogenetic protein-signaling pathway in human ovarian surface epithelium and ovarian cancer cells. Endocrinology. 144:2003;3306-3314
    • (2003) Endocrinology , vol.144 , pp. 3306-3314
    • Shepherd, T.G.1    Nachtigal, M.W.2
  • 12
    • 0036399170 scopus 로고    scopus 로고
    • Extracellular regulation of BMP signaling in vertebrates: A cocktail of modulators
    • Balemans W., Van Hul W. Extracellular regulation of BMP signaling in vertebrates: a cocktail of modulators. Dev. Biol. 250:2002;231-250
    • (2002) Dev. Biol. , vol.250 , pp. 231-250
    • Balemans, W.1    Van Hul, W.2
  • 13
    • 0033538447 scopus 로고    scopus 로고
    • Id genes are direct targets of bone morphogenetic protein induction in embryonic stem cells
    • Hollnagel A., Oehlmann V., Heymer J., Ruther U., Nordheim A. Id genes are direct targets of bone morphogenetic protein induction in embryonic stem cells. J. Biol. Chem. 274:1999;19838-19845
    • (1999) J. Biol. Chem. , vol.274 , pp. 19838-19845
    • Hollnagel, A.1    Oehlmann, V.2    Heymer, J.3    Ruther, U.4    Nordheim, A.5
  • 15
    • 0037085441 scopus 로고    scopus 로고
    • Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter
    • Korchynskyi, ten Dijke P. Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter. J. Biol. Chem. 277:2002;4883-4891
    • (2002) J. Biol. Chem. , vol.277 , pp. 4883-4891
    • Korchynskyi1    Ten Dijke, P.2
  • 16
    • 0141557542 scopus 로고    scopus 로고
    • Regulation of TGF-β signaling by protein inhibitor of activated STAT, PIASy through Smad3
    • Imoto S., Sugiyama K., Muromoto R., Sato N., Yamamoto T., Matsuda T. Regulation of TGF-β signaling by protein inhibitor of activated STAT, PIASy through Smad3. J. Biol. Chem. 278:2003;34253-34258
    • (2003) J. Biol. Chem. , vol.278 , pp. 34253-34258
    • Imoto, S.1    Sugiyama, K.2    Muromoto, R.3    Sato, N.4    Yamamoto, T.5    Matsuda, T.6
  • 17
    • 0034657917 scopus 로고    scopus 로고
    • Modulation of STAT signaling by STAT-interacting proteins
    • Shuai K. Modulation of STAT signaling by STAT-interacting proteins. Oncogene. 19:2000;2638-2644
    • (2000) Oncogene , vol.19 , pp. 2638-2644
    • Shuai, K.1
  • 19
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of Stat3 signal transduction by PIAS3
    • Chung C.D., Liao J., Liu B., Rao X., Jay P., Berta P., Shuai K. Specific inhibition of Stat3 signal transduction by PIAS3. Science. 278:1997;1803-1805
    • (1997) Science , vol.278 , pp. 1803-1805
    • Chung, C.D.1    Liao, J.2    Liu, B.3    Rao, X.4    Jay, P.5    Berta, P.6    Shuai, K.7
  • 20
    • 0034530046 scopus 로고    scopus 로고
    • ARIP3 androgen receptor-interacting protein 3 and other PIAS protein inhibitor of activated STAT proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation
    • Kotaja N., Aittomaki S., Silvennoinen O., Palvimo J.J., Janne O.A. ARIP3 androgen receptor-interacting protein 3 and other PIAS protein inhibitor of activated STAT proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation. Mol. Endocrinol. 14:2000;1986-2000
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1986-2000
    • Kotaja, N.1    Aittomaki, S.2    Silvennoinen, O.3    Palvimo, J.J.4    Janne, O.A.5
  • 22
    • 0035963311 scopus 로고    scopus 로고
    • Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells
    • Gross M., Liu B., Tan J., French F.S., Carey M., Shuai K. Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells. Oncogene. 20:2001;3880-3887
    • (2001) Oncogene , vol.20 , pp. 3880-3887
    • Gross, M.1    Liu, B.2    Tan, J.3    French, F.S.4    Carey, M.5    Shuai, K.6
  • 23
    • 0035576737 scopus 로고    scopus 로고
    • A new RING for SUMO: Wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases
    • Jackson P.K. A new RING for SUMO: wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases. Genes Dev. 15:2001;3053-3058
    • (2001) Genes Dev. , vol.15 , pp. 3053-3058
    • Jackson, P.K.1
  • 24
    • 0034789730 scopus 로고    scopus 로고
    • Involvement of PIAS1 in the sumoylation of tumor suppressor p53
    • Kahyo T., Nishida T., Yasuda H. Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell. 8:2001;713-718
    • (2001) Mol. Cell , vol.8 , pp. 713-718
    • Kahyo, T.1    Nishida, T.2    Yasuda, H.3
  • 25
    • 0035024007 scopus 로고    scopus 로고
    • A putative protein inhibitor of activated STAT PIASy interacts with p53 and inhibits p53-mediated transactivation but not apoptosis
    • Nelson V., Davis G.E., Maxwell S.A. A putative protein inhibitor of activated STAT PIASy interacts with p53 and inhibits p53-mediated transactivation but not apoptosis. Apoptosis. 6:2001;221-234
    • (2001) Apoptosis , vol.6 , pp. 221-234
    • Nelson, V.1    Davis, G.E.2    Maxwell, S.A.3
  • 26
    • 0035576878 scopus 로고    scopus 로고
    • PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
    • Sachdev S., Bruhn L., Sieber H., Pichler A., Melchior F., Grosschedl R. PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes Dev. 15:2001;3088-3103
    • (2001) Genes Dev. , vol.15 , pp. 3088-3103
    • Sachdev, S.1    Bruhn, L.2    Sieber, H.3    Pichler, A.4    Melchior, F.5    Grosschedl, R.6
  • 27
    • 0038558190 scopus 로고    scopus 로고
    • Sumoylation is involved in beta-catenin-dependent activation of Tcf-4
    • Yamamoto H., Ihara M., Matsuura Y., Kikuchi A. Sumoylation is involved in beta-catenin-dependent activation of Tcf-4. EMBO J. 22:2003;2047-2059
    • (2003) EMBO J. , vol.22 , pp. 2047-2059
    • Yamamoto, H.1    Ihara, M.2    Matsuura, Y.3    Kikuchi, A.4
  • 28
    • 0043194033 scopus 로고    scopus 로고
    • Repression of Smad transcriptional activity by PIASy, an inhibitor of activated STAT
    • Long J., Matsuura I., He D., Wang G., Shuai K., Liu F. Repression of Smad transcriptional activity by PIASy, an inhibitor of activated STAT. Proc. Natl. Acad. Sci. USA. 100:2003;9791-9796
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9791-9796
    • Long, J.1    Matsuura, I.2    He, D.3    Wang, G.4    Shuai, K.5    Liu, F.6
  • 29
    • 0032528041 scopus 로고    scopus 로고
    • Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors
    • Kawabata M., Inoue H., Hanyu A., Imamura T., Miyazono K. Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors. EMBO J. 17:1998;4056-4065
    • (1998) EMBO J. , vol.17 , pp. 4056-4065
    • Kawabata, M.1    Inoue, H.2    Hanyu, A.3    Imamura, T.4    Miyazono, K.5
  • 31
    • 0028894025 scopus 로고
    • Disruption of transforming growth factor beta signaling by a mutation that prevents transphosphorylation within the receptor complex
    • Carcamo J., Zentella A., Massagué J. Disruption of transforming growth factor beta signaling by a mutation that prevents transphosphorylation within the receptor complex. Mol. Cell. Biol. 15:1995;1573-1581
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1573-1581
    • Carcamo, J.1    Zentella, A.2    Massagué, J.3
  • 32
    • 0035813135 scopus 로고    scopus 로고
    • DJ-1 Positively regulates the androgen receptor by impairing the binding of PIASxα to the receptor
    • Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M., Ariga H. DJ-1 Positively regulates the androgen receptor by impairing the binding of PIASxα to the receptor. J. Biol. Chem. 276:2001;37556-37563
    • (2001) J. Biol. Chem. , vol.276 , pp. 37556-37563
    • Takahashi, K.1    Taira, T.2    Niki, T.3    Seino, C.4    Iguchi-Ariga, S.M.5    Ariga, H.6
  • 33
    • 0034725044 scopus 로고    scopus 로고
    • SOCS-1 can suppress CD3ζ- and Syk-mediated NF-AT activation in a non-lymphoid cell line
    • Matsuda T., Yamamoto T., Kishi H., Yoshimura A., Muraguchi A. SOCS-1 can suppress CD3ζ- and Syk-mediated NF-AT activation in a non-lymphoid cell line. FEBS Lett. 47:2000;235-240
    • (2000) FEBS Lett. , vol.47 , pp. 235-240
    • Matsuda, T.1    Yamamoto, T.2    Kishi, H.3    Yoshimura, A.4    Muraguchi, A.5
  • 35
    • 0037443154 scopus 로고    scopus 로고
    • Induction of C/EBPα activity alters gene expression and differentiation of human CD34+ cells
    • Cammenga J., Mulloy J.C., Berguido F.J., MacGrogan D., Viale A., Nimer S.D. Induction of C/EBPα activity alters gene expression and differentiation of human CD34+ cells. Blood. 101:2003;2206-2214
    • (2003) Blood , vol.101 , pp. 2206-2214
    • Cammenga, J.1    Mulloy, J.C.2    Berguido, F.J.3    MacGrogan, D.4    Viale, A.5    Nimer, S.D.6
  • 36
    • 0035943676 scopus 로고    scopus 로고
    • Activation of Estrogen receptor blocks interleukin-6-inducible cell growth of human multiple myeloma involving molecular cross-talk between estrogen receptor and STAT3 mediated by co-regulator PIAS3
    • Wang L.H., Yang X.Y., Mihalic K., Xiao W., Li D., Farrar W.L. Activation of Estrogen receptor blocks interleukin-6-inducible cell growth of human multiple myeloma involving molecular cross-talk between estrogen receptor and STAT3 mediated by co-regulator PIAS3. J. Biol. Chem. 276:2001;31839-31844
    • (2001) J. Biol. Chem. , vol.276 , pp. 31839-31844
    • Wang, L.H.1    Yang, X.Y.2    Mihalic, K.3    Xiao, W.4    Li, D.5    Farrar, W.L.6
  • 37
    • 0031859380 scopus 로고    scopus 로고
    • A novel pathway for mammary epithelial cell invasion induced by the helix-loop-helix protein Id-1
    • Desprez P.Y., Lin C.Q., Thomasset N., Sympson C.J., Bissell M.J., Campisi J. A novel pathway for mammary epithelial cell invasion induced by the helix-loop-helix protein Id-1. Mol. Cell. Biol. 18:1998;4577-4588
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4577-4588
    • Desprez, P.Y.1    Lin, C.Q.2    Thomasset, N.3    Sympson, C.J.4    Bissell, M.J.5    Campisi, J.6
  • 38
    • 0031923282 scopus 로고    scopus 로고
    • Coupling of cell growth control and apoptosis functions of Id proteins
    • Norton J.D., Atherton G.T. Coupling of cell growth control and apoptosis functions of Id proteins. Mol. Cell. Biol. 18:1998;2371-2381
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2371-2381
    • Norton, J.D.1    Atherton, G.T.2
  • 39
    • 0032566633 scopus 로고    scopus 로고
    • Forced expression of Id-1 in the adult mouse small intestinal epithelium is associated with development of adenomas
    • Wice B.M., Gordon J.I. Forced expression of Id-1 in the adult mouse small intestinal epithelium is associated with development of adenomas. J. Biol. Chem. 273:1998;25310-25319
    • (1998) J. Biol. Chem. , vol.273 , pp. 25310-25319
    • Wice, B.M.1    Gordon, J.I.2
  • 40
  • 41
    • 0036283061 scopus 로고    scopus 로고
    • Cross-talk between bone morphogenetic proteins and estrogen receptor signaling
    • Yamamoto T., Saatcioglu F., Matsuda T. Cross-talk between bone morphogenetic proteins and estrogen receptor signaling. Endocrinology. 143:2002;2635-2642
    • (2002) Endocrinology , vol.143 , pp. 2635-2642
    • Yamamoto, T.1    Saatcioglu, F.2    Matsuda, T.3
  • 42
    • 0035336677 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Hay R.T. Protein modification by SUMO. Trends Biochem. Sci. 26:2001;332-333
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 332-333
    • Hay, R.T.1
  • 43
    • 0035032914 scopus 로고    scopus 로고
    • Divergence and convergence of TGF-β/BMP signaling
    • Miyazono K., Kusanagi K., Inoue H. Divergence and convergence of TGF-β/BMP signaling. J. Cell Physiol. 187:2001;265-276
    • (2001) J. Cell Physiol. , vol.187 , pp. 265-276
    • Miyazono, K.1    Kusanagi, K.2    Inoue, H.3
  • 44
    • 0037862003 scopus 로고    scopus 로고
    • New intracellular components of bone morphogenetic protein/Smad signaling cascades
    • Zwijsen A., Verschueren K., Huylebroeck D. New intracellular components of bone morphogenetic protein/Smad signaling cascades. FEBS Lett. 546:2003;133-139
    • (2003) FEBS Lett. , vol.546 , pp. 133-139
    • Zwijsen, A.1    Verschueren, K.2    Huylebroeck, D.3
  • 45
    • 0033549789 scopus 로고    scopus 로고
    • A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation
    • Zhu H., Kavsak P., Abdollah S., Wrana J.L., Thomsen G.H. A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature. 400:1999;687-693
    • (1999) Nature , vol.400 , pp. 687-693
    • Zhu, H.1    Kavsak, P.2    Abdollah, S.3    Wrana, J.L.4    Thomsen, G.H.5
  • 46
    • 0034711290 scopus 로고    scopus 로고
    • Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor- signaling
    • Lin X., Liang M., Feng X.H. Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor- signaling. J. Biol. Chem. 275:2000;36818-36822
    • (2000) J. Biol. Chem. , vol.275 , pp. 36818-36822
    • Lin, X.1    Liang, M.2    Feng, X.H.3
  • 47
    • 0035918274 scopus 로고    scopus 로고
    • Smurf1 interacts with transforming growth factor-β type I receptor through Smad7 and induces receptor degradation
    • Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K. Smurf1 interacts with transforming growth factor-β type I receptor through Smad7 and induces receptor degradation. J. Biol. Chem. 276:2001;12477-12480
    • (2001) J. Biol. Chem. , vol.276 , pp. 12477-12480
    • Ebisawa, T.1    Fukuchi, M.2    Murakami, G.3    Chiba, T.4    Tanaka, K.5    Imamura, T.6    Miyazono, K.7
  • 48
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-β receptor for degradation
    • Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-β receptor for degradation. Mol. Cell. 6:2000;1365-1375
    • (2000) Mol. Cell , vol.6 , pp. 1365-1375
    • Kavsak, P.1    Rasmussen, R.K.2    Causing, C.G.3    Bonni, S.4    Zhu, H.5    Thomsen, G.H.6    Wrana, J.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.