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Volumn 92, Issue 4, 1998, Pages 1199-1205

Multiple forms of the SH2-containing inositol phosphatase, SHIP, are generated by C-terminal truncation

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; GLUTATHIONE TRANSFERASE; HEMAGGLUTININ; INOSITOL PHOSPHATASE; INTERLEUKIN 3; PHOSPHATASE; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 0032529325     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v92.4.1199     Document Type: Article
Times cited : (56)

References (34)
  • 1
    • 0029978202 scopus 로고    scopus 로고
    • The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
    • Damen JE, Liu L, Rosten P, Humphries RK, Jefferson AB, Majerus PW, Krystal G: The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Proc Natl Acad Sci USA 93:1689, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1689
    • Damen, J.E.1    Liu, L.2    Rosten, P.3    Humphries, R.K.4    Jefferson, A.B.5    Majerus, P.W.6    Krystal, G.7
  • 3
    • 0028888604 scopus 로고
    • The PTB domain: A new protein module implicated in signal transduction
    • Van der Geer P, Pawson T: The PTB domain: A new protein module implicated in signal transduction. Trends Biochem Sci 20:277, 1995
    • (1995) Trends Biochem Sci , vol.20 , pp. 277
    • Van der Geer, P.1    Pawson, T.2
  • 4
    • 0028961785 scopus 로고
    • Properties of type II inositol polyphosphate 5-phosphatase
    • Jefferson AB. Majerus PW: Properties of type II inositol polyphosphate 5-phosphatase. J Biol Chem 270:9370, 1995
    • (1995) J Biol Chem , vol.270 , pp. 9370
    • Jefferson, A.B.1    Majerus, P.W.2
  • 6
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker A, Cantley LC: Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature 387:673, 1997
    • (1997) Nature , vol.387 , pp. 673
    • Toker, A.1    Cantley, L.C.2
  • 9
    • 0030975468 scopus 로고    scopus 로고
    • The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis
    • Liu L, Damen JE, Hughes MR, Babic I, Jirik FR, Krystal G: The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis. J Biol Chem 272:8983, 1997
    • (1997) J Biol Chem , vol.272 , pp. 8983
    • Liu, L.1    Damen, J.E.2    Hughes, M.R.3    Babic, I.4    Jirik, F.R.5    Krystal, G.6
  • 10
    • 0030892128 scopus 로고    scopus 로고
    • Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2
    • Liu L, Damen JE, Ware MD, Krystal G: Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2. J Biol Chem 272:10998, 1997
    • (1997) J Biol Chem , vol.272 , pp. 10998
    • Liu, L.1    Damen, J.E.2    Ware, M.D.3    Krystal, G.4
  • 14
    • 0027324057 scopus 로고
    • Molecular cloning of the mouse grb2 gene: Differential interaction of the Grb2 adaptor protein with epidermal growth factor and nerve growth factor receptors
    • Suen K-L, Bustelo XR, Pawson T, Barbacid M: Molecular cloning of the mouse grb2 gene: Differential interaction of the Grb2 adaptor protein with epidermal growth factor and nerve growth factor receptors. Mol Cell Biol 13:5500, 1993
    • (1993) Mol Cell Biol , vol.13 , pp. 5500
    • Suen, K.-L.1    Bustelo, X.R.2    Pawson, T.3    Barbacid, M.4
  • 15
    • 0029067403 scopus 로고
    • PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine
    • Kavanaugh WM, Turck CW, Williams LT: PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 268:1177, 1995
    • (1995) Science , vol.268 , pp. 1177
    • Kavanaugh, W.M.1    Turck, C.W.2    Williams, L.T.3
  • 16
    • 0028385758 scopus 로고
    • Versatile retroviral vectors for potential use in gene therapy
    • Hawley RG, Lieu FHL, Fong AZC, Hawley TS: Versatile retroviral vectors for potential use in gene therapy. Gene Ther 1:136, 1994 .
    • (1994) Gene Ther , vol.1 , pp. 136
    • Hawley, R.G.1    Fhl, L.2    Azc, F.3    Hawley, T.S.4
  • 17
    • 0027360189 scopus 로고
    • Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein
    • Damen JE, Liu L, Cutler RL, Krystal G: Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein. Blood 82:2296, 1993
    • (1993) Blood , vol.82 , pp. 2296
    • Damen, J.E.1    Liu, L.2    Cutler, R.L.3    Krystal, G.4
  • 18
    • 0028041512 scopus 로고
    • Multiple cytokines stimulate the binding of a common 145-kilodalton protein to Shc at the Grb2 recognition site of Shc
    • Liu L, Damen JE, Cutler RL, Krystal G: Multiple cytokines stimulate the binding of a common 145-kilodalton protein to Shc at the Grb2 recognition site of Shc. Mol Cell Biol 14:6926, 1994
    • (1994) Mol Cell Biol , vol.14 , pp. 6926
    • Liu, L.1    Damen, J.E.2    Cutler, R.L.3    Krystal, G.4
  • 19
    • 0028876287 scopus 로고
    • Src homologous and collagen (Shc) protein binds to F-actin and translocates to the cytoskeleton upon nerve growth factor stimulation in PC12 cells
    • Thomas D, Patterson SD, Bradshaw RA: Src homologous and collagen (Shc) protein binds to F-actin and translocates to the cytoskeleton upon nerve growth factor stimulation in PC12 cells. J Biol Chem 270:28924, 1995
    • (1995) J Biol Chem , vol.270 , pp. 28924
    • Thomas, D.1    Patterson, S.D.2    Bradshaw, R.A.3
  • 20
    • 0031000904 scopus 로고    scopus 로고
    • Purification and molecular cloning of SH2- And SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl
    • Odai H, Sasaki K, Iwamatsu A, Nakamoto T, Ueno H, Yamagata T, Mitani K, Yazaki Y, Hirai H: Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl, Blood 89:2745, 1997
    • (1997) Blood , vol.89 , pp. 2745
    • Odai, H.1    Sasaki, K.2    Iwamatsu, A.3    Nakamoto, T.4    Ueno, H.5    Yamagata, T.6    Mitani, K.7    Yazaki, Y.8    Hirai, H.9
  • 21
    • 0019983285 scopus 로고
    • Interaction of platelet-derived growth factor with its fibroblast receptor. Demonstration of ligand degradation and receptor modulation
    • Heldin CH, Wasteson A, Westermark B: Interaction of platelet-derived growth factor with its fibroblast receptor. Demonstration of ligand degradation and receptor modulation. J Biol Chem 257:4216, 1982
    • (1982) J Biol Chem , vol.257 , pp. 4216
    • Ch, H.1    Wasteson, A.2    Westermark, B.3
  • 22
    • 0029937677 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin: A central role for elasto-lactacystin beta-lactone
    • Dick LR, Cruikshank AA, Grenier L, Melandri FD, Nunes SL, Stein RL: Mechanistic studies on the inactivation of the proteasome by lactacystin: A central role for elasto-lactacystin beta-lactone. J Biol Chem 271:7273, 1996
    • (1996) J Biol Chem , vol.271 , pp. 7273
    • Dick, L.R.1    Cruikshank, A.A.2    Grenier, L.3    Melandri, F.D.4    Nunes, S.L.5    Stein, R.L.6
  • 23
    • 0030472889 scopus 로고    scopus 로고
    • Different interleukin-1 beta converting enzyme (ICE) family protease requirements for the apoptotic death of T lymphocytes triggered by diverse stimuli
    • Sarin A, Wu M-L, Henkart PA: Different interleukin-1 beta converting enzyme (ICE) family protease requirements for the apoptotic death of T lymphocytes triggered by diverse stimuli. J Exp Med 184:2445, 1996
    • (1996) J Exp Med , vol.184 , pp. 2445
    • Sarin, A.1    Wu, M.-L.2    Henkart, P.A.3
  • 26
    • 0029859565 scopus 로고    scopus 로고
    • Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation
    • Ware MD, Rosten P, Damen JE, Liu L, Humphries RK, Krystal G: Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation. Blood 88:2833, 1996
    • (1996) Blood , vol.88 , pp. 2833
    • Ware, M.D.1    Rosten, P.2    Damen, J.E.3    Liu, L.4    Humphries, R.K.5    Krystal, G.6
  • 27
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteoiysis
    • Rechsteiner M, Rogers SW: PEST sequences and regulation by proteoiysis. Trends Biochem Sci 21:267, 1996
    • (1996) Trends Biochem Sci , vol.21 , pp. 267
    • Rechsteiner, M.1    Rogers, S.W.2
  • 28
    • 0028088153 scopus 로고
    • Calpain: New perspectives in molecular diversity and physiological-pathological involvement
    • Saido TC, Sorimachi H, Suzuki K: Calpain: New perspectives in molecular diversity and physiological-pathological involvement. FASEB 18:814, 1994
    • (1994) FASEB , vol.18 , pp. 814
    • Saido, T.C.1    Sorimachi, H.2    Suzuki, K.3
  • 31
    • 0029959174 scopus 로고    scopus 로고
    • A novel phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase associates with the interleukin-3 receptor
    • Liu L, Jefferson AB, Zhang X, Noms FA, Majerus PW, Krystal G: A novel phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase associates with the interleukin-3 receptor. J Biol Chem 271:29729, 1996
    • (1996) J Biol Chem , vol.271 , pp. 29729
    • Liu, L.1    Jefferson, A.B.2    Zhang, X.3    Noms, F.A.4    Majerus, P.W.5    Krystal, G.6
  • 32
    • 0030890880 scopus 로고    scopus 로고
    • Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets
    • Norris FA, Atkins RC, Majerus PW: Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets. J Biol Chem 272:10987, 1997
    • (1997) J Biol Chem , vol.272 , pp. 10987
    • Norris, F.A.1    Atkins, R.C.2    Majerus, P.W.3
  • 33
    • 0026695689 scopus 로고
    • Replacement of m-calpain by mu-calpain during maturation of megakaryocytes and possible involvement in platelet formation
    • Nakamura M, Mori M, Nakazawa S, Tange T, Hayashi M, Saito Y, Kawashima S: Replacement of m-calpain by mu-calpain during maturation of megakaryocytes and possible involvement in platelet formation. Thromb Res 66:757, 1992
    • (1992) Thromb Res , vol.66 , pp. 757
    • Nakamura, M.1    Mori, M.2    Nakazawa, S.3    Tange, T.4    Hayashi, M.5    Saito, Y.6    Kawashima, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.