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Volumn 97, Issue 2 SPEC. ISS., 2005, Pages 235-243

The p95-100 kDa ligand of the T cell-specific adaptor (TSAd) protein Src-homology-2 (SH2) domain implicated in TSAd nuclear import is p97 Valosin-containing protein (VCP)

Author keywords

Nuclear import; SH2; Signal transduction; T cell; TSAd; VCP

Indexed keywords

ISOPROTEIN; LIGAND; PROTEIN; PROTEIN P95; PROTEIN P97; PROTEIN SH2; PROTEIN TYROSINE KINASE; T CELL SPECIFIC ADAPTOR PROTEIN; T LYMPHOCYTE RECEPTOR; TYROSINE; UNCLASSIFIED DRUG; VALOSIN CONTAINING PROTEIN;

EID: 14744269010     PISSN: 01652478     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imlet.2004.10.021     Document Type: Conference Paper
Times cited : (19)

References (40)
  • 1
    • 0032548933 scopus 로고    scopus 로고
    • Molecular cloning of a T cell-specific adapter protein (TSAd) containing an Src homology (SH) 2 domain and putative SH3 and phosphotyrosine binding sites
    • A. Spurkland, J.E. Brinchmann, G. Markussen, F. Pedeutour, E. Munthe, T. Lea, F. Vartdal, and H.C. Aasheim Molecular cloning of a T cell-specific adapter protein (TSAd) containing an Src homology (SH) 2 domain and putative SH3 and phosphotyrosine binding sites J Biol Chem 273 1998 4539 4546
    • (1998) J Biol Chem , vol.273 , pp. 4539-4546
    • Spurkland, A.1    Brinchmann, J.E.2    Markussen, G.3    Pedeutour, F.4    Munthe, E.5    Lea, T.6    Vartdal, F.7    Aasheim, H.C.8
  • 2
    • 0003477424 scopus 로고    scopus 로고
    • An adapter protein interacting with the SH2 domain of p56lck, is required for T cell activation
    • Y.B. Choi, C.K. Kim, and Y.Y. Lad An adapter protein interacting with the SH2 domain of p56lck, is required for T cell activation J Immunol 163 1999 5242 5249
    • (1999) J Immunol , vol.163 , pp. 5242-5249
    • Choi, Y.B.1    Kim, C.K.2    Lad, Y.Y.3
  • 4
    • 0035908033 scopus 로고    scopus 로고
    • A transcription function for the T cell-specific adapter (TSAd) protein in T cells: Critical role of the TSAd Src homology 2 domain
    • F. Marti, N.H. Post, E. Chan, and P.D. King A transcription function for the T cell-specific adapter (TSAd) protein in T cells: critical role of the TSAd Src homology 2 domain J Exp Med 193 2001 1425 1430
    • (2001) J Exp Med , vol.193 , pp. 1425-1430
    • Marti, F.1    Post, N.H.2    Chan, E.3    King, P.D.4
  • 5
    • 0042886906 scopus 로고    scopus 로고
    • Impaired T cell death and lupus-like autoimmunity in T cell-specific adapter protein-deficient mice
    • J. Drappa, L.A. Kamen, E. Chan, M. Georgiev, D. Ashany, F. Marti, and P.D. King Impaired T cell death and lupus-like autoimmunity in T cell-specific adapter protein-deficient mice J Exp Med 198 2003 809 821
    • (2003) J Exp Med , vol.198 , pp. 809-821
    • Drappa, J.1    Kamen, L.A.2    Chan, E.3    Georgiev, M.4    Ashany, D.5    Marti, F.6    King, P.D.7
  • 7
    • 0037378478 scopus 로고    scopus 로고
    • MEK kinase 2 and the adaptor protein Lad regulate extracellular signal-regulated kinase 5 activation by epidermal growth factor via Src
    • W. Sun, X. Wei, K. Kesavan, T.P. Garrington, R. Fan, J. Mei, S.M. Anderson, E.W. Gelfand, and G.L. Johnson MEK kinase 2 and the adaptor protein Lad regulate extracellular signal-regulated kinase 5 activation by epidermal growth factor via Src Mol Cell Biol 23 2003 2298 2308
    • (2003) Mol Cell Biol , vol.23 , pp. 2298-2308
    • Sun, W.1    Wei, X.2    Kesavan, K.3    Garrington, T.P.4    Fan, R.5    Mei, J.6    Anderson, S.M.7    Gelfand, E.W.8    Johnson, G.L.9
  • 8
    • 0036315121 scopus 로고    scopus 로고
    • Disruption of Mekk2 in mice reveals an unexpected role for MEKK2 in modulating T-cell receptor signal transduction
    • Z. Guo, G. Clydesdale, J. Cheng, K. Kim, L. Gan, D.J. McConkey, S.E. Ullrich, Y. Zhuang, and B. Su Disruption of Mekk2 in mice reveals an unexpected role for MEKK2 in modulating T-cell receptor signal transduction Mol Cell Biol 22 2002 5761 5768
    • (2002) Mol Cell Biol , vol.22 , pp. 5761-5768
    • Guo, Z.1    Clydesdale, G.2    Cheng, J.3    Kim, K.4    Gan, L.5    McConkey, D.J.6    Ullrich, S.E.7    Zhuang, Y.8    Su, B.9
  • 9
    • 0242635839 scopus 로고    scopus 로고
    • P97, a protein coping with multiple identities
    • P.G. Woodman p97, a protein coping with multiple identities J Cell Sci 116 2003 4283 4290
    • (2003) J Cell Sci , vol.116 , pp. 4283-4290
    • Woodman, P.G.1
  • 10
    • 1642309633 scopus 로고    scopus 로고
    • Molecular perspectives on p97-VCP: Progress in understanding its structure and diverse biological functions
    • Q. Wang, C. Song, and C.C. Li Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions J Struct Biol 146 2004 44 57
    • (2004) J Struct Biol , vol.146 , pp. 44-57
    • Wang, Q.1    Song, C.2    Li, C.C.3
  • 11
    • 0032578519 scopus 로고    scopus 로고
    • LCK-phosphorylated human killer cell-inhibitory receptors recruit and activate phosphatidylinositol 3-kinase
    • F. Marti, C.W. Xu, A. Selvakumar, R. Brent, B. Dupont, and P.D. King LCK-phosphorylated human killer cell-inhibitory receptors recruit and activate phosphatidylinositol 3-kinase Proc Natl Acad Sci U S A 95 1998 11810 11815
    • (1998) Proc Natl Acad Sci U S a , vol.95 , pp. 11810-11815
    • Marti, F.1    Xu, C.W.2    Selvakumar, A.3    Brent, R.4    Dupont, B.5    King, P.D.6
  • 12
    • 0035159453 scopus 로고    scopus 로고
    • Negative-feedback regulation of CD28 costimulation by a novel mitogen-activated protein kinase phosphatase, MKP6
    • F. Marti, A. Krause, N.H. Post, C. Lyddane, B. Dupont, M. Sadelain, and P.D. King Negative-feedback regulation of CD28 costimulation by a novel mitogen-activated protein kinase phosphatase, MKP6 J Immunol 166 2001 197 206
    • (2001) J Immunol , vol.166 , pp. 197-206
    • Marti, F.1    Krause, A.2    Post, N.H.3    Lyddane, C.4    Dupont, B.5    Sadelain, M.6    King, P.D.7
  • 13
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • M. Latterich, K.U. Frohlich, and R. Schekman Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes Cell 82 1995 885 893
    • (1995) Cell , vol.82 , pp. 885-893
    • Latterich, M.1    Frohlich, K.U.2    Schekman, R.3
  • 14
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • J. Kuriyan, and D. Cowburn Modular peptide recognition domains in eukaryotic signaling Annu Rev Biophys Biomol Struct 26 1997 259 288
    • (1997) Annu Rev Biophys Biomol Struct , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 15
    • 0028587687 scopus 로고
    • Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver
    • L. Zhang, C.L. Ashendel, G.W. Becker, and D.J. Morre Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver J Cell Biol 127 1994 1871 1883
    • (1994) J Cell Biol , vol.127 , pp. 1871-1883
    • Zhang, L.1    Ashendel, C.L.2    Becker, G.W.3    Morre, D.J.4
  • 16
    • 0020120095 scopus 로고
    • Cold-sensitive cell-division-cycle mutants of yeast: Isolation, properties, and pseudoreversion studies
    • D. Moir, S.E. Stewart, B.C. Osmond, and D. Botstein Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies Genetics 100 1982 547 563
    • (1982) Genetics , vol.100 , pp. 547-563
    • Moir, D.1    Stewart, S.E.2    Osmond, B.C.3    Botstein, D.4
  • 17
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • R.M. Dai, and C.C. Li Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation Nat Cell Biol 3 2001 740 744
    • (2001) Nat Cell Biol , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.C.2
  • 18
    • 0033451992 scopus 로고    scopus 로고
    • Synergistic roles for Pim-1 and c-Myc in STAT3-mediated cell cycle progression and antiapoptosis
    • T. Shirogane, T. Fukada, J.M. Muller, D.T. Shima, M. Hibi, and T. Hirano Synergistic roles for Pim-1 and c-Myc in STAT3-mediated cell cycle progression and antiapoptosis Immunity 11 1999 709 719
    • (1999) Immunity , vol.11 , pp. 709-719
    • Shirogane, T.1    Fukada, T.2    Muller, J.M.3    Shima, D.T.4    Hibi, M.5    Hirano, T.6
  • 19
    • 0032968207 scopus 로고    scopus 로고
    • C. elegans MAC-1, an essential member of the AAA family of ATPases, can bind CED-4 and prevent cell death
    • D. Wu, P.J. Chen, S. Chen, Y. Hu, G. Nunez, and R.E. Ellis C. elegans MAC-1, an essential member of the AAA family of ATPases, can bind CED-4 and prevent cell death Development 126 1999 2021 2031
    • (1999) Development , vol.126 , pp. 2021-2031
    • Wu, D.1    Chen, P.J.2    Chen, S.3    Hu, Y.4    Nunez, G.5    Ellis, R.E.6
  • 20
    • 0043066575 scopus 로고    scopus 로고
    • Cold-inducible expression of the cell division cycle gene CDC48 and its promotion of cell proliferation during cold acclimation in zebrafish cells
    • S. Imamura, N. Ojima, and M. Yamashita Cold-inducible expression of the cell division cycle gene CDC48 and its promotion of cell proliferation during cold acclimation in zebrafish cells FEBS Lett. 549 2003 14 20
    • (2003) FEBS Lett. , vol.549 , pp. 14-20
    • Imamura, S.1    Ojima, N.2    Yamashita, M.3
  • 21
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with IkBa and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkBa
    • R.M. Dai, E. Chen, D.L. Longo, C.M. Gorbea, and C.C. Li Involvement of valosin-containing protein, an ATPase co-purified with IkBa and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkBa J Biol Chem 273 1998 3562 3573
    • (1998) J Biol Chem , vol.273 , pp. 3562-3573
    • Dai, R.M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.C.5
  • 22
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
    • M. Rape, T. Hoppe, I. Gorr, M. Kalocay, H. Richly, and S. Jentsch Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone Cell 107 2001 667 677
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 23
    • 0038376459 scopus 로고    scopus 로고
    • Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90
    • N. Shcherbik, T. Zoladek, J.T. Nickels, and D.S. Haines Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90 Curr Biol 13 2003 1227 1233
    • (2003) Curr Biol , vol.13 , pp. 1227-1233
    • Shcherbik, N.1    Zoladek, T.2    Nickels, J.T.3    Haines, D.S.4
  • 24
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • H.H. Meyer, J.G. Shorter, J. Seemann, D. Pappin, and G. Warren A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways EMBO J 19 2000 2181 2192
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 25
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Y. Ye, H.H. Meyer, and T.A. Rapoport The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol Nature 414 2001 652 656
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 26
    • 0036704679 scopus 로고    scopus 로고
    • Protein dislocation from the endoplasmic reticulum-pulling out the suspect
    • E. Jarosch, R. Geiss-Friedlander, B. Meusser, J. Walter, and T. Sommer Protein dislocation from the endoplasmic reticulum-pulling out the suspect Traffic 3 2002 530 556
    • (2002) Traffic , vol.3 , pp. 530-556
    • Jarosch, E.1    Geiss-Friedlander, R.2    Meusser, B.3    Walter, J.4    Sommer, T.5
  • 27
    • 0026660330 scopus 로고
    • VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation
    • M. Egerton, O.R. Ashe, D. Chen, B.J. Druker, W.H. Burgess, and L.E. Samelson VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation EMBO J 11 1992 3533 3540
    • (1992) EMBO J , vol.11 , pp. 3533-3540
    • Egerton, M.1    Ashe, O.R.2    Chen, D.3    Druker, B.J.4    Burgess, W.H.5    Samelson, L.E.6
  • 28
    • 0028237892 scopus 로고
    • Biochemical characterization of valosin-containing protein, a protein tyrosine kinase substrate in hematopoietic cells
    • M. Egerton, and L.E. Samelson Biochemical characterization of valosin-containing protein, a protein tyrosine kinase substrate in hematopoietic cells J Biol Chem 269 1994 11435 11441
    • (1994) J Biol Chem , vol.269 , pp. 11435-11441
    • Egerton, M.1    Samelson, L.E.2
  • 29
    • 0031932987 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p
    • F. Madeo, J. Schlauer, H. Zischka, D. Mecke, and K.U. Frohlich Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p Mol Biol Cell 9 1998 131 141
    • (1998) Mol Biol Cell , vol.9 , pp. 131-141
    • Madeo, F.1    Schlauer, J.2    Zischka, H.3    Mecke, D.4    Frohlich, K.U.5
  • 30
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • N. Blom, S. Gammeltoft, and S. Brunak Sequence and structure-based prediction of eukaryotic protein phosphorylation sites J Mol Biol 294 1999 1351 1362
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 34
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • B. DeLaBarre, and A.T. Brunger Complete structure of p97/valosin- containing protein reveals communication between nucleotide domains Nat Struct Biol 10 2003 856 863
    • (2003) Nat Struct Biol , vol.10 , pp. 856-863
    • Delabarre, B.1    Brunger, A.T.2
  • 37
    • 0040293484 scopus 로고    scopus 로고
    • The mouse p97 (CDC48) gene, Genomic structure, definition of transcriptional regulatory sequences, gene expression, and characterization of a pseudogene
    • J.M. Muller, H.H. Meyer, C. Ruhrberg, G.W. Stamp, G. Warren, and D.T. Shima The mouse p97 (CDC48) gene, Genomic structure, definition of transcriptional regulatory sequences, gene expression, and characterization of a pseudogene J Biol Chem 274 1999 10154 10162
    • (1999) J Biol Chem , vol.274 , pp. 10154-10162
    • Muller, J.M.1    Meyer, H.H.2    Ruhrberg, C.3    Stamp, G.W.4    Warren, G.5    Shima, D.T.6
  • 38
    • 0033855808 scopus 로고    scopus 로고
    • VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells
    • H. Zhang, Q. Wang, K. Kajino, and M.I. Greene VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells DNA Cell Biol 19 2000 253 263
    • (2000) DNA Cell Biol , vol.19 , pp. 253-263
    • Zhang, H.1    Wang, Q.2    Kajino, K.3    Greene, M.I.4
  • 39
    • 0141764739 scopus 로고    scopus 로고
    • DNA damage modulates nucleolar interaction of the Werner protein with the AAA ATPase p97/VCP
    • J.J. Partridge, J.O. Lopreiato Jr., M. Latterich, and F.E. Indig DNA damage modulates nucleolar interaction of the Werner protein with the AAA ATPase p97/VCP Mol Biol Cell 14 2003 4221 4229
    • (2003) Mol Biol Cell , vol.14 , pp. 4221-4229
    • Partridge, J.J.1    Lopreiato Jr., J.O.2    Latterich, M.3    Indig, F.E.4
  • 40
    • 0035947238 scopus 로고    scopus 로고
    • The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II
    • A. Ferdous, F. Gonzalez, L. Sun, T. Kodadek, and S.A. Johnston The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II Mol Cell 7 2001 981 991
    • (2001) Mol Cell , vol.7 , pp. 981-991
    • Ferdous, A.1    Gonzalez, F.2    Sun, L.3    Kodadek, T.4    Johnston, S.A.5


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