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Volumn 386, Issue 1, 2009, Pages 242-246

CHIP functions an E3 ubiquitin ligase of Runx1

Author keywords

CHIP Stub1; Degradation; Hsp70 90 chaperone; Runx1; Ubiquitination

Indexed keywords

CHAPERONE; CYCLOHEXIMIDE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEIN; PROTEIN STUB1; TRANSCRIPTION FACTOR RUNX1; TRANSCRIPTION FACTOR RUNX2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 67649220617     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.06.043     Document Type: Article
Times cited : (48)

References (26)
  • 1
    • 0027220003 scopus 로고
    • PEBP2/PEA2 represents a family of transcription factors homologous to the products of the Drosophila runt gene and the human AML1 gene
    • Ogawa E., Maruyama M., Kagoshima H., Inuzuka M., Lu J., Satake M., Shigesada K., and Ito Y. PEBP2/PEA2 represents a family of transcription factors homologous to the products of the Drosophila runt gene and the human AML1 gene. Proc. Natl. Acad. Sci. USA 90 (1993) 6859-6863
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6859-6863
    • Ogawa, E.1    Maruyama, M.2    Kagoshima, H.3    Inuzuka, M.4    Lu, J.5    Satake, M.6    Shigesada, K.7    Ito, Y.8
  • 3
    • 23044463578 scopus 로고    scopus 로고
    • Runx1 prevents wasting, myofibrillar disorganization, and autophagy of skeletal muscle
    • Wang X., Blagden C., Fan J., Nowak S.J., Taniuchi I., Littman D.R., and Burden S.J. Runx1 prevents wasting, myofibrillar disorganization, and autophagy of skeletal muscle. Genes Dev. 19 (2005) 1715-1722
    • (2005) Genes Dev. , vol.19 , pp. 1715-1722
    • Wang, X.1    Blagden, C.2    Fan, J.3    Nowak, S.J.4    Taniuchi, I.5    Littman, D.R.6    Burden, S.J.7
  • 4
    • 31444439049 scopus 로고    scopus 로고
    • A role for Runx transcription factor signaling in dorsal root ganglion sensory neuron diversification
    • Kramer I., Sigrist M., de Nooij J.C., Taniuchi I., Jessell T.M., and Arber S. A role for Runx transcription factor signaling in dorsal root ganglion sensory neuron diversification. Neuron 49 (2006) 379-393
    • (2006) Neuron , vol.49 , pp. 379-393
    • Kramer, I.1    Sigrist, M.2    de Nooij, J.C.3    Taniuchi, I.4    Jessell, T.M.5    Arber, S.6
  • 5
    • 0030061554 scopus 로고    scopus 로고
    • AML1, the target of multiple chromosomal translocations in human leukemia, is essential for normal fetal liver hematopoiesis
    • Okuda T., van Deursen J., Hiebert S.W., Grosveld G., and Downing J.R. AML1, the target of multiple chromosomal translocations in human leukemia, is essential for normal fetal liver hematopoiesis. Cell 84 (1996) 321-330
    • (1996) Cell , vol.84 , pp. 321-330
    • Okuda, T.1    van Deursen, J.2    Hiebert, S.W.3    Grosveld, G.4    Downing, J.R.5
  • 6
    • 0036636857 scopus 로고    scopus 로고
    • Core-binding factors in haematopoiesis and leukaemia
    • Speck N.A., and Gilliland D.G. Core-binding factors in haematopoiesis and leukaemia. Nat. Rev. Cancer 2 (2002) 502-513
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 502-513
    • Speck, N.A.1    Gilliland, D.G.2
  • 9
    • 8944230662 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase pathway phosphorylates AML1, an acute myeloid leukemia gene product, and potentially regulates its transactivation ability
    • Tanaka T., Kurokawa M., Ueki K., Tanaka K., Imai Y., Mitani K., Okazaki K., Sagata N., Yazaki Y., Shibata Y., Kadowaki T., and Hirai H. The extracellular signal-regulated kinase pathway phosphorylates AML1, an acute myeloid leukemia gene product, and potentially regulates its transactivation ability. Mol. Cell. Biol. 16 (1996) 3967-3979
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3967-3979
    • Tanaka, T.1    Kurokawa, M.2    Ueki, K.3    Tanaka, K.4    Imai, Y.5    Mitani, K.6    Okazaki, K.7    Sagata, N.8    Yazaki, Y.9    Shibata, Y.10    Kadowaki, T.11    Hirai, H.12
  • 12
    • 33749643800 scopus 로고    scopus 로고
    • AML1/RUNX1 phosphorylation by cyclin-dependent kinases regulates the degradation of AML1/RUNX1 by the anaphase-promoting complex
    • Biggs J.R., Peterson L.F., Zhang Y., Kraft A.S., and Zhang D.E. AML1/RUNX1 phosphorylation by cyclin-dependent kinases regulates the degradation of AML1/RUNX1 by the anaphase-promoting complex. Mol. Cell. Biol. 26 (2006) 7420-7429
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7420-7429
    • Biggs, J.R.1    Peterson, L.F.2    Zhang, Y.3    Kraft, A.S.4    Zhang, D.E.5
  • 13
    • 0035865459 scopus 로고    scopus 로고
    • Dimerization with PEBP2beta protects RUNX1/AML1 from ubiquitin-proteasome-mediated degradation
    • Huang G., Shigesada K., Ito K., Wee H.J., Yokomizo T., and Ito Y. Dimerization with PEBP2beta protects RUNX1/AML1 from ubiquitin-proteasome-mediated degradation. EMBO J. 20 (2001) 723-733
    • (2001) EMBO J. , vol.20 , pp. 723-733
    • Huang, G.1    Shigesada, K.2    Ito, K.3    Wee, H.J.4    Yokomizo, T.5    Ito, Y.6
  • 14
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.Y., and Patterson C. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 19 (1999) 4535-4545
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 15
    • 0037039327 scopus 로고    scopus 로고
    • Protein turnover: a CHIP programmed for proteolysis
    • Wiederkehr T., Bukau B., and Buchberger A. Protein turnover: a CHIP programmed for proteolysis. Curr. Biol. 12 (2002) R26-R28
    • (2002) Curr. Biol. , vol.12
    • Wiederkehr, T.1    Bukau, B.2    Buchberger, A.3
  • 16
    • 33645293437 scopus 로고    scopus 로고
    • CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70
    • Qian S.B., McDonough H., Boellmann F., Cyr D.M., and Patterson C. CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70. Nature 440 (2006) 551-555
    • (2006) Nature , vol.440 , pp. 551-555
    • Qian, S.B.1    McDonough, H.2    Boellmann, F.3    Cyr, D.M.4    Patterson, C.5
  • 17
    • 20144385807 scopus 로고    scopus 로고
    • CHIP controls the sensitivity of TGF-b signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradation
    • Xin H., Xu X., Li L., Ning H., Rong Y., Shang Y., Wang Y., Fu X.-Y., and Chang Z. CHIP controls the sensitivity of TGF-b signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradation. J. Biol. Chem. 280 (2005) 20842-20850
    • (2005) J. Biol. Chem. , vol.280 , pp. 20842-20850
    • Xin, H.1    Xu, X.2    Li, L.3    Ning, H.4    Rong, Y.5    Shang, Y.6    Wang, Y.7    Fu, X.-Y.8    Chang, Z.9
  • 18
    • 35548989214 scopus 로고    scopus 로고
    • Differential ubiquitination of Smad1 mediated by CHIP: implications in the regulation of the bone morphogenetic protein signaling pathway
    • Li R.F., Shang Y., Liu D., Ren Z.S., Chang Z., and Sui S.F. Differential ubiquitination of Smad1 mediated by CHIP: implications in the regulation of the bone morphogenetic protein signaling pathway. J. Mol. Biol. 374 (2007) 777-790
    • (2007) J. Mol. Biol. , vol.374 , pp. 777-790
    • Li, R.F.1    Shang, Y.2    Liu, D.3    Ren, Z.S.4    Chang, Z.5    Sui, S.F.6
  • 21
    • 0031940065 scopus 로고    scopus 로고
    • Intrinsic transcriptional activation-inhibition domains of the polyomavirus enhancer binding protein 2/core binding factor alpha subunit revealed in the presence of the beta subunit
    • Kanno T., Kanno Y., Chen L.F., Ogawa E., Kim W.Y., and Ito Y. Intrinsic transcriptional activation-inhibition domains of the polyomavirus enhancer binding protein 2/core binding factor alpha subunit revealed in the presence of the beta subunit. Mol. Cell. Biol. 18 (1998) 2444-2454
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2444-2454
    • Kanno, T.1    Kanno, Y.2    Chen, L.F.3    Ogawa, E.4    Kim, W.Y.5    Ito, Y.6
  • 22
    • 4744348809 scopus 로고    scopus 로고
    • Notch-induced E2A degradation requires CHIP and Hsc70 as novel facilitators of ubiquitination
    • Huang Z., Nie L., Xu M., and Sun X.H. Notch-induced E2A degradation requires CHIP and Hsc70 as novel facilitators of ubiquitination. Mol. Cell. Biol. 24 (2004) 8951-8962
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8951-8962
    • Huang, Z.1    Nie, L.2    Xu, M.3    Sun, X.H.4
  • 23
    • 0041845297 scopus 로고    scopus 로고
    • E3 ubiquitin ligase Smurf1 mediates core-binding factor alpha1/Runx2 degradation and plays a specific role in osteoblast differentiation
    • Zhao M., Qiao M., Oyajobi B.O., Mundy G.R., and Chen D. E3 ubiquitin ligase Smurf1 mediates core-binding factor alpha1/Runx2 degradation and plays a specific role in osteoblast differentiation. J. Biol. Chem. 278 (2003) 27939-27944
    • (2003) J. Biol. Chem. , vol.278 , pp. 27939-27944
    • Zhao, M.1    Qiao, M.2    Oyajobi, B.O.3    Mundy, G.R.4    Chen, D.5
  • 24
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: a quality-control E3 ligase collaborating with molecular chaperones
    • Murata S., Chiba T., and Tanaka K. CHIP: a quality-control E3 ligase collaborating with molecular chaperones. Int. J. Biochem. Cell. Biol. 35 (2003) 572-578
    • (2003) Int. J. Biochem. Cell. Biol. , vol.35 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 25
    • 39549106043 scopus 로고    scopus 로고
    • CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins
    • Parsons J.L., Tait P.S., Finch D., Dianova II, Allinson S.L., and Dianov G.L. CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins. Mol. Cell 29 (2008) 477-487
    • (2008) Mol. Cell , vol.29 , pp. 477-487
    • Parsons, J.L.1    Tait, P.S.2    Finch, D.3    Dianova II4    Allinson, S.L.5    Dianov, G.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.