메뉴 건너뛰기




Volumn 319, Issue 2, 2004, Pages 683-689

Pak regulates calpain-dependent degradation of E3b1

Author keywords

Calpain; E3b1; Pak; Rac; Serum starvation

Indexed keywords

CALPAIN; PROTEIN DERIVATIVE; PROTEIN E3B1; PROTEIN PAK; UNCLASSIFIED DRUG;

EID: 2642574097     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.05.042     Document Type: Article
Times cited : (3)

References (31)
  • 4
    • 0027957728 scopus 로고
    • The GRB2/Sem-5 adaptor protein
    • Downward J. The GRB2/Sem-5 adaptor protein. FEBS Lett. 338:1994;113-117
    • (1994) FEBS Lett. , vol.338 , pp. 113-117
    • Downward, J.1
  • 5
    • 0030014704 scopus 로고    scopus 로고
    • Sos1 rapidly associates with Grb2 and is hypophosphorylated when complexed with the EGF receptor after EGF stimulation
    • Hu Y., Bowtell D.D. Sos1 rapidly associates with Grb2 and is hypophosphorylated when complexed with the EGF receptor after EGF stimulation. Oncogene. 12:1996;1865-1872
    • (1996) Oncogene , vol.12 , pp. 1865-1872
    • Hu, Y.1    Bowtell, D.D.2
  • 6
    • 0028844631 scopus 로고
    • Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity
    • Shi Y., Alin K., Goff S.P. Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity. Genes Dev. 9:1995;2583-2597
    • (1995) Genes Dev. , vol.9 , pp. 2583-2597
    • Shi, Y.1    Alin, K.2    Goff, S.P.3
  • 7
    • 0031032916 scopus 로고    scopus 로고
    • Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth
    • Biesova Z., Piccoli C., Wong W.T. Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth. Oncogene. 14:1997;233-241
    • (1997) Oncogene , vol.14 , pp. 233-241
    • Biesova, Z.1    Piccoli, C.2    Wong, W.T.3
  • 8
    • 0033796315 scopus 로고    scopus 로고
    • Abl interactor 1 binds to sos and inhibits epidermal growth factor- and v-Abl-induced activation of extracellular signal-regulated kinases
    • Fan P.D., Goff S.P. Abl interactor 1 binds to sos and inhibits epidermal growth factor- and v-Abl-induced activation of extracellular signal-regulated kinases. Mol. Cell. Biol. 20:2000;7591-7601
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7591-7601
    • Fan, P.D.1    Goff, S.P.2
  • 9
    • 0032523919 scopus 로고    scopus 로고
    • Oncogenic Abl and Src tyrosine kinases elicit the ubiquitin-dependent degradation of target proteins through a Ras-independent pathway
    • Dai Z., Quackenbush R.C., Courtney K.D., Grove M., Cortez D., Reuther G.W., Pendergast A.M. Oncogenic Abl and Src tyrosine kinases elicit the ubiquitin-dependent degradation of target proteins through a Ras-independent pathway. Genes Dev. 12:1998;1415-1424
    • (1998) Genes Dev. , vol.12 , pp. 1415-1424
    • Dai, Z.1    Quackenbush, R.C.2    Courtney, K.D.3    Grove, M.4    Cortez, D.5    Reuther, G.W.6    Pendergast, A.M.7
  • 10
    • 0035800802 scopus 로고    scopus 로고
    • Deletion of the Src homology 3 domain and C-terminal proline-rich sequences in Bcr-Abl prevents Abl interactor 2 degradation and spontaneous cell migration and impairs leukemogenesis
    • Dai Z., Kerzic P., Schroeder W.G., McNiece I.K. Deletion of the Src homology 3 domain and C-terminal proline-rich sequences in Bcr-Abl prevents Abl interactor 2 degradation and spontaneous cell migration and impairs leukemogenesis. J. Biol. Chem. 276:2001;28954-28960
    • (2001) J. Biol. Chem. , vol.276 , pp. 28954-28960
    • Dai, Z.1    Kerzic, P.2    Schroeder, W.G.3    McNiece, I.K.4
  • 11
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M., Rogers S.W. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21:1996;267-271
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 12
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S., Wells R., Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science. 234:1986;364-368
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 13
    • 0025875671 scopus 로고
    • Natural substrates of the ubiquitin proteolytic pathway
    • Rechsteiner M. Natural substrates of the ubiquitin proteolytic pathway. Cell. 66:1991;615-618
    • (1991) Cell , vol.66 , pp. 615-618
    • Rechsteiner, M.1
  • 14
    • 0028886219 scopus 로고
    • PEST sequences in calmodulin-binding proteins
    • Barnes J.A., Gomes A.V. PEST sequences in calmodulin-binding proteins. Mol. Cell. Biochem. 149-150:1995;17-27
    • (1995) Mol. Cell. Biochem. , vol.149-150 , pp. 17-27
    • Barnes, J.A.1    Gomes, A.V.2
  • 15
    • 0032748298 scopus 로고    scopus 로고
    • Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity
    • Zenke F.T., King C.C., Bohl B.P., Bokoch G.M. Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity. J. Biol. Chem. 274:1999;32565-32573
    • (1999) J. Biol. Chem. , vol.274 , pp. 32565-32573
    • Zenke, F.T.1    King, C.C.2    Bohl, B.P.3    Bokoch, G.M.4
  • 16
    • 0035816539 scopus 로고    scopus 로고
    • BetaPix-enhanced p38 activation by Cdc42/Rac/PAK/MKK3/6-mediated pathway. Implication in the regulation of membrane ruffling
    • Lee S.H., Eom M., Lee S.J., Kim S., Park H.J., Park D. BetaPix-enhanced p38 activation by Cdc42/Rac/PAK/MKK3/6-mediated pathway. Implication in the regulation of membrane ruffling. J. Biol. Chem. 276:2001;25066-25072
    • (2001) J. Biol. Chem. , vol.276 , pp. 25066-25072
    • Lee, S.H.1    Eom, M.2    Lee, S.J.3    Kim, S.4    Park, H.J.5    Park, D.6
  • 17
    • 0032559962 scopus 로고    scopus 로고
    • Epidermal growth factor activation of NF-kappaB is mediated through IkappaBalpha degradation and intracellular free calcium
    • Sun L., Carpenter G. Epidermal growth factor activation of NF-kappaB is mediated through IkappaBalpha degradation and intracellular free calcium. Oncogene. 16:1998;2095-2102
    • (1998) Oncogene , vol.16 , pp. 2095-2102
    • Sun, L.1    Carpenter, G.2
  • 18
    • 0034680918 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme a reductase
    • Ravid T., Doolman R., Avner R., Harats D., Roitelman J. The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 275:2000;35840-35847
    • (2000) J. Biol. Chem. , vol.275 , pp. 35840-35847
    • Ravid, T.1    Doolman, R.2    Avner, R.3    Harats, D.4    Roitelman, J.5
  • 19
    • 0029830139 scopus 로고    scopus 로고
    • The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1
    • Galisteo M.L., Chernoff J., Su Y.C., Skolnik E.Y., Schlessinger J. The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1. J. Biol. Chem. 271:1996;20997-21000
    • (1996) J. Biol. Chem. , vol.271 , pp. 20997-21000
    • Galisteo, M.L.1    Chernoff, J.2    Su, Y.C.3    Skolnik, E.Y.4    Schlessinger, J.5
  • 21
    • 0029949921 scopus 로고    scopus 로고
    • The role of calpastatin (the specific calpain inhibitor) in myoblast differentiation and fusion
    • Barnoy S., Glasner T., Kosower N.S. The role of calpastatin (the specific calpain inhibitor) in myoblast differentiation and fusion. Biochem. Biophys. Res. Commun. 220:1996;933-938
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 933-938
    • Barnoy, S.1    Glasner, T.2    Kosower, N.S.3
  • 23
    • 0024561590 scopus 로고
    • Intracellular regulatory system involving calpain and calpastatin
    • Murachi T. Intracellular regulatory system involving calpain and calpastatin. Biochem. Int. 18:1989;263-294
    • (1989) Biochem. Int. , vol.18 , pp. 263-294
    • Murachi, T.1
  • 24
    • 0028088153 scopus 로고
    • Calpain: New perspectives in molecular diversity and physiological- pathological involvement
    • Saido T.C., Sorimachi H., Suzuki K. Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J. 8:1994;814-822
    • (1994) FASEB J. , vol.8 , pp. 814-822
    • Saido, T.C.1    Sorimachi, H.2    Suzuki, K.3
  • 27
    • 0031021491 scopus 로고    scopus 로고
    • Cyclic GMP-dependent protein kinase and cellular signaling in the nervous system
    • Wang X., Robinson P.J. Cyclic GMP-dependent protein kinase and cellular signaling in the nervous system. J. Neurochem. 68:1997;443-456
    • (1997) J. Neurochem. , vol.68 , pp. 443-456
    • Wang, X.1    Robinson, P.J.2
  • 28
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: Calpain proteases in cell motility
    • Glading A., Lauffenburger D.A., Wells A. Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol. 12:2002;46-54
    • (2002) Trends Cell Biol. , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.