메뉴 건너뛰기




Volumn 93, Issue 6, 1999, Pages 2013-2024

Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp

Author keywords

[No Author keywords available]

Indexed keywords

PHYTOHEMAGGLUTININ; PROTEIN KINASE; PROTEIN TYROSINE PHOSPHATASE; T LYMPHOCYTE RECEPTOR;

EID: 0033559313     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v93.6.2013.406k25_2013_2024     Document Type: Article
Times cited : (284)

References (66)
  • 1
    • 0026712410 scopus 로고
    • Great expectations: Protein tyrosine phosphatases in cell regulation
    • Brautigan DL: Great expectations: Protein tyrosine phosphatases in cell regulation. Biochem Biophys Acta 1114:63, 1992
    • (1992) Biochem Biophys Acta , vol.1114 , pp. 63
    • Brautigan, D.L.1
  • 2
    • 0023611733 scopus 로고
    • The approaching era of the tumor suppressor genes
    • Klein G: The approaching era of the tumor suppressor genes. Science 238:1539, 1987
    • (1987) Science , vol.238 , pp. 1539
    • Klein, G.1
  • 5
    • 0026324171 scopus 로고
    • Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes
    • Fischer EH, Charbonneau H, Tonks HK: Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes. Science 253:401, 1991
    • (1991) Science , vol.253 , pp. 401
    • Fischer, E.H.1    Charbonneau, H.2    Tonks, H.K.3
  • 6
    • 0025146562 scopus 로고
    • Structural diversity and evolution of human receptor-like protein tyrosine phosphatases
    • Kruegert NX, Streuli M, Saito H: Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J 9:3241, 1990
    • (1990) EMBO J , vol.9 , pp. 3241
    • Kruegert, N.X.1    Streuli, M.2    Saito, H.3
  • 7
    • 0030297552 scopus 로고    scopus 로고
    • From form to function: Signaling by protein tyrosine phosphatases
    • Tonks NK, Neel BG: From form to function: Signaling by protein tyrosine phosphatases. Cell 87:365, 1996
    • (1996) Cell , vol.87 , pp. 365
    • Tonks, N.K.1    Neel, B.G.2
  • 8
    • 0029125639 scopus 로고
    • Protein tyrosine phosphatases as adhesion receptors
    • Brady-Kanlnay SM, Tonks NK: Protein tyrosine phosphatases as adhesion receptors. Curr Opin Cell Biol 7:650, 1995
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 650
    • Brady-Kanlnay, S.M.1    Tonks, N.K.2
  • 9
    • 0026584285 scopus 로고
    • The non-transmembrane tyrosine phosphatase PTP-1B localized to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • Frangioni JV, Beahm PH, Shifirin V, Jost CA, Neel BGL: The non-transmembrane tyrosine phosphatase PTP-1B localized to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell 68:545, 1992
    • (1992) Cell , vol.68 , pp. 545
    • Frangioni, J.V.1    Beahm, P.H.2    Shifirin, V.3    Jost, C.A.4    Neel, B.G.L.5
  • 10
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T: Protein modules and signalling networks. Nature 323:573, 1995
    • (1995) Nature , vol.323 , pp. 573
    • Pawson, T.1
  • 11
    • 0028277983 scopus 로고
    • Nuclear localization of the PEP protein tyrosine phosphatase
    • Flores E, Roy G, Patel D, Shaw A, Thomas ML: Nuclear localization of the PEP protein tyrosine phosphatase. Mol Cell Biol 14:4938, 1994
    • (1994) Mol Cell Biol , vol.14 , pp. 4938
    • Flores, E.1    Roy, G.2    Patel, D.3    Shaw, A.4    Thomas, M.L.5
  • 12
    • 0026742211 scopus 로고
    • Characterization of hematopoietic intracellular protein tyrosine phosphatases: Description of phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences
    • Matthews RJ, Bowne DB, Flores E, Thomas ML: Characterization of hematopoietic intracellular protein tyrosine phosphatases: Description of phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. Mol Cell Biol 12:2396, 1992
    • (1992) Mol Cell Biol , vol.12 , pp. 2396
    • Matthews, R.J.1    Bowne, D.B.2    Flores, E.3    Thomas, M.L.4
  • 13
    • 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
  • 14
    • 0030796443 scopus 로고    scopus 로고
    • csk is associated with protein-tyrosine phosphatase PTP-PEST in hemopoietic and non-hemopoietic cells
    • csk is associated with protein-tyrosine phosphatase PTP-PEST in hemopoietic and non-hemopoietic cells. J Biol Chem 272:23455, 1997
    • (1997) J Biol Chem , vol.272 , pp. 23455
    • Davidson, D.1    Cloutier, J.F.2    Gregorieff, A.3    Veillette, A.4
  • 15
    • 0029819526 scopus 로고    scopus 로고
    • CSK with protein tyrosine phosphatase PEP in T cells and other hematopoietic cells
    • CSK with protein tyrosine phosphatase PEP in T cells and other hematopoietic cells. EMBO J 15:4909, 1996
    • (1996) EMBO J , vol.15 , pp. 4909
    • Cloutier, J.F.1    Veillette, A.2
  • 16
    • 0024327898 scopus 로고
    • The leukocyte common antigen family
    • Thomas ML: The leukocyte common antigen family. Annu Rev Immunol 7:339, 1989
    • (1989) Annu Rev Immunol , vol.7 , pp. 339
    • Thomas, M.L.1
  • 17
    • 0025898888 scopus 로고
    • Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45
    • Justement LB, Campbell KS, Chien NC, Cambier JC: Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45. Science 252:1839, 1991
    • (1991) Science , vol.252 , pp. 1839
    • Justement, L.B.1    Campbell, K.S.2    Chien, N.C.3    Cambier, J.C.4
  • 18
    • 0024416009 scopus 로고
    • Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation
    • Pingel JT, Thomas ML: Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation. Cell 58:1055, 1989
    • (1989) Cell , vol.58 , pp. 1055
    • Pingel, J.T.1    Thomas, M.L.2
  • 22
    • 0027488637 scopus 로고
    • Hematopoietic cell phosphatase associates with the interleukin (IL-3) receptor beta chain and down regulates IL-3-induced tyrosine phosphorylation and mitogenesis
    • Yi T, Mui AL, Krystal G, Ihle JN: Hematopoietic cell phosphatase associates with the interleukin (IL-3) receptor beta chain and down regulates IL-3-induced tyrosine phosphorylation and mitogenesis. Mol Cell Biol 13:7577, 1993
    • (1993) Mol Cell Biol , vol.13 , pp. 7577
    • Yi, T.1    Mui, A.L.2    Krystal, G.3    Ihle, J.N.4
  • 23
    • 0029904324 scopus 로고    scopus 로고
    • lck phosphorylation and ZAP-70 binding to T cell receptor ζ chain
    • lck phosphorylation and ZAP-70 binding to T cell receptor ζ chain. Biochem Biophys Res Commun 222:50, 1996
    • (1996) Biochem Biophys Res Commun , vol.222 , pp. 50
    • Raab, M.1    Rudd, C.E.2
  • 24
    • 0027195626 scopus 로고
    • Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene
    • Tsui HW, Siminovitch KA, Souza L, Tsui FWL: Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nat Genet 4:124, 1993
    • (1993) Nat Genet , vol.4 , pp. 124
    • Tsui, H.W.1    Siminovitch, K.A.2    Souza, L.3    Tsui, F.W.L.4
  • 25
    • 0026593420 scopus 로고
    • Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase)
    • Zanke B, Suzuki H, Kishihara K, Mizzen L, Minden M, Pawson A, MakTW: Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase). Eur J Immunol 22:253, 1992
    • (1992) Eur J Immunol , vol.22 , pp. 253
    • Zanke, B.1    Suzuki, H.2    Kishihara, K.3    Mizzen, L.4    Minden, M.5    Pawson, A.6    Mak, T.W.7
  • 26
    • 0028027169 scopus 로고
    • The protein product of the c-cbl proto-oncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor
    • Donovan JA, Wange RL, Lagdon WY, Samelson LE: The protein product of the c-cbl proto-oncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor. J Biol Chem 269:22921, 1994
    • (1994) J Biol Chem , vol.269 , pp. 22921
    • Donovan, J.A.1    Wange, R.L.2    Lagdon, W.Y.3    Samelson, L.E.4
  • 29
    • 0026580912 scopus 로고
    • Rapid physical mapping of cloned DNA on banded mouse chromosomes by fluorescence in situ hybridization
    • Boyle AL, Feltquite DM, Dracopoli NC, Housman DE, Ward DC: Rapid physical mapping of cloned DNA on banded mouse chromosomes by fluorescence in situ hybridization. Genomics 12:106, 1992
    • (1992) Genomics , vol.12 , pp. 106
    • Boyle, A.L.1    Feltquite, D.M.2    Dracopoli, N.C.3    Housman, D.E.4    Ward, D.C.5
  • 30
    • 0027225483 scopus 로고
    • Modes of DAPI banding and simultaneous in situ hybridization
    • Heng H, Tsui LC: Modes of DAPI banding and simultaneous in situ hybridization. Chromosoma 102:325, 1993
    • (1993) Chromosoma , vol.102 , pp. 325
    • Heng, H.1    Tsui, L.C.2
  • 31
    • 0027947017 scopus 로고
    • Digitized and differentially shaded human chromosome idegrams for genomic applications
    • Francke U: Digitized and differentially shaded human chromosome idegrams for genomic applications. Cytogene Cell Genet 65:206, 1994
    • (1994) Cytogene Cell Genet , vol.65 , pp. 206
    • Francke, U.1
  • 32
    • 0025046879 scopus 로고
    • The effects of leukemia inhibitory factor (LIF) on the blast stem cells of acute myeloblastic leukemia
    • Wang C, Lishner M, Minden MD, McCulloch EA: The effects of leukemia inhibitory factor (LIF) on the blast stem cells of acute myeloblastic leukemia. Leukemia 4:548, 1990
    • (1990) Leukemia , vol.4 , pp. 548
    • Wang, C.1    Lishner, M.2    Minden, M.D.3    McCulloch, E.A.4
  • 34
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp TP, Woods KR: Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 78:3824, 1993
    • (1993) Proc Natl Acad Sci USA , vol.78 , pp. 3824
    • Hopp, T.P.1    Woods, K.R.2
  • 35
    • 0025865103 scopus 로고
    • A Tyr/Ser protein phosphatase encoded by vacinia virus
    • Guan K, Broyles SS, Dixon JE: A Tyr/Ser protein phosphatase encoded by vacinia virus. Nature 350:359, 1991
    • (1991) Nature , vol.350 , pp. 359
    • Guan, K.1    Broyles, S.S.2    Dixon, J.E.3
  • 36
    • 0024378995 scopus 로고
    • A family of receptor linked protein tyrosine phosphatases in humans and Drosophila
    • Stueli M, Krueger NX, Tsai AYM, Saito H: A family of receptor linked protein tyrosine phosphatases in humans and Drosophila. Proc Natl Acad Sci USA 86:3698, 1989
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3698
    • Stueli, M.1    Krueger, N.X.2    Tsai, A.Y.M.3    Saito, H.4
  • 37
    • 0027184496 scopus 로고
    • Cloning and expression of PTP-PEST. A novel, human, non-transmembrane protein tyrosine phosphatase
    • Yang Q, Co D, Sommercorn J, Tonks NK: Cloning and expression of PTP-PEST. A novel, human, non-transmembrane protein tyrosine phosphatase. J Biol Chem 268:17650, 1993
    • (1993) J Biol Chem , vol.268 , pp. 17650
    • Yang, Q.1    Co, D.2    Sommercorn, J.3    Tonks, N.K.4
  • 38
    • 0023924803 scopus 로고
    • Purification of the major protein tyrosine phosphatases of human placenta
    • Tonks NK, Diltz CD, Fischer EH: Purification of the major protein tyrosine phosphatases of human placenta. J Biol Chem 263: 6722, 1988
    • (1988) J Biol Chem , vol.263 , pp. 6722
    • Tonks, N.K.1    Diltz, C.D.2    Fischer, E.H.3
  • 40
    • 0025992880 scopus 로고
    • Identification, cloning, and expression of a cytosolic megakaryocyte protein tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1
    • Gu M, York JD, Warshawsky I, Majerus PW: Identification, cloning, and expression of a cytosolic megakaryocyte protein tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1 Proc Natl Acad Sci USA 88:5867, 1991
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5867
    • Gu, M.1    York, J.D.2    Warshawsky, I.3    Majerus, P.W.4
  • 41
    • 0022552131 scopus 로고
    • Point mutation define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak M: Point mutation define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44:283, 1986
    • (1986) Cell , vol.44 , pp. 283
    • Kozak, M.1
  • 42
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen GB, Ren R, Baltimore D: Modular binding domains in signal transduction proteins. Cell 80:237, 1995
    • (1995) Cell , vol.80 , pp. 237
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 43
    • 0030049298 scopus 로고    scopus 로고
    • Affinity, specificity, and kinetics of the interaction of the SHC phosphotyrosine binding domain with asparagine-X-X-phosphotyrosine motifs of growth factor receptors
    • Laminet AA, Apell G, Conroy L, Kavanaugh WM: Affinity, specificity, and kinetics of the interaction of the SHC phosphotyrosine binding domain with asparagine-X-X-phosphotyrosine motifs of growth factor receptors. J Biol Chem 271:264, 1996
    • (1996) J Biol Chem , vol.271 , pp. 264
    • Laminet, A.A.1    Apell, G.2    Conroy, L.3    Kavanaugh, W.M.4
  • 44
    • 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 234:364, 1986
    • (1986) Science , vol.234 , pp. 364
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 45
    • 0025856538 scopus 로고
    • The C terminus of mouse ornithine decarboxylase confers rapid degradation on dihydrofolate reductase. Support for the pest hypothesis
    • Loescher P, Pratt G, Rechsteiner M: The C terminus of mouse ornithine decarboxylase confers rapid degradation on dihydrofolate reductase. Support for the pest hypothesis. J Bio Chem 266:11213, 1991
    • (1991) J Bio Chem , vol.266 , pp. 11213
    • Loescher, P.1    Pratt, G.2    Rechsteiner, M.3
  • 46
    • 0029007116 scopus 로고
    • Murine tyrosine phosphatase PEST, a stable cytosolic protein tyrosine phosphtase
    • Charest A, Wagner J, Shen SH, Tremblay ML: Murine tyrosine phosphatase PEST, a stable cytosolic protein tyrosine phosphtase. Biochem J 308:425, 1995
    • (1995) Biochem J , vol.308 , pp. 425
    • Charest, A.1    Wagner, J.2    Shen, S.H.3    Tremblay, M.L.4
  • 54
    • 0027257623 scopus 로고
    • Cloning and expression of two structurally distinct receptor-linked protein-tyrosine phosphatases generated by RNA processing from a single gene
    • Pan MG, Rim C, Lu KP, Florio T, Stork PJS: Cloning and expression of two structurally distinct receptor-linked protein-tyrosine phosphatases generated by RNA processing from a single gene. J Biol Chem 268:19284, 1993
    • (1993) J Biol Chem , vol.268 , pp. 19284
    • Pan, M.G.1    Rim, C.2    Lu, Kp.3    Florio, T.4    Stork, P.J.S.5
  • 55
    • 0027522709 scopus 로고
    • Alternative splicing gives rise to a nuclear protein tyrosine phoshatase in Drosophila
    • McLaughlin S, Dixon JE: Alternative splicing gives rise to a nuclear protein tyrosine phoshatase in Drosophila. J Biol Chem 268:6839, 1993
    • (1993) J Biol Chem , vol.268 , pp. 6839
    • McLaughlin, S.1    Dixon, J.E.2
  • 56
    • 0029563428 scopus 로고
    • Alternative splicing generates four different forms of a non-transmembrane protein tyrosine phosphatase mRNA
    • Reddy RS, Swarup G: Alternative splicing generates four different forms of a non-transmembrane protein tyrosine phosphatase mRNA. DNA Cell Biol 14:1007, 1995
    • (1995) DNA Cell Biol , vol.14 , pp. 1007
    • Reddy, R.S.1    Swarup, G.2
  • 57
    • 0029998593 scopus 로고    scopus 로고
    • Two splice variants of thyrosine phosphatase differ in substrate specificity, DNA binding, and subcellular location
    • Kamatkar S, Radha V, Nambirajan S, Reddy RS, Swarup G: Two splice variants of thyrosine phosphatase differ in substrate specificity, DNA binding, and subcellular location. J Biol Chem 271:26755, 1996
    • (1996) J Biol Chem , vol.271 , pp. 26755
    • Kamatkar, S.1    Radha, V.2    Nambirajan, S.3    Reddy, R.S.4    Swarup, G.5
  • 58
    • 0028180211 scopus 로고
    • RNA splicing regulates the activity of a SH2 domain-containing protein tyrosine phosphatase
    • Mei L, Doherty CA, Huganir RL: RNA splicing regulates the activity of a SH2 domain-containing protein tyrosine phosphatase. J Biol Chem 269:12254, 1994
    • (1994) J Biol Chem , vol.269 , pp. 12254
    • Mei, L.1    Doherty, C.A.2    Huganir, R.L.3
  • 59
    • 0025265082 scopus 로고
    • Identification of major nucleolar proteins as candidate of cdc2 kinase
    • Peter MJ, Nakagawa M, Dorée M, Labbé JC, Nigg EA: Identification of major nucleolar proteins as candidate of cdc2 kinase. Cell 60:791, 1990
    • (1990) Cell , vol.60 , pp. 791
    • Peter, M.J.1    Nakagawa, M.2    Dorée, M.3    Labbé, J.C.4    Nigg, E.A.5
  • 60
    • 0026006392 scopus 로고
    • cdc2 kinase activation in vertebrates
    • cdc2 kinase activation in vertebrates. EMBO J 10:3331, 1991
    • (1991) EMBO J , vol.10 , pp. 3331
    • Krek, W.1    Nigg, E.A.2
  • 61
    • 0030889218 scopus 로고    scopus 로고
    • The product of the proto-oncogene c-cbl a negative regulator of the Syk tyrosine kinase
    • Ota Y, Samelson LE: The product of the proto-oncogene c-cbl a negative regulator of the Syk tyrosine kinase. Science 276:418, 1997
    • (1997) Science , vol.276 , pp. 418
    • Ota, Y.1    Samelson, L.E.2
  • 62
    • 14444276991 scopus 로고    scopus 로고
    • The Cbl phosphotyrsine-binding domain select a D(N/ D)XpY motif and bind to the Tyr292 negative regulatory phosphorylating site of ZAP-70
    • Lupher ML Jr, Songyang Z, Songyang Z, Shoelson SE, Cantley LC, Band H: The Cbl phosphotyrsine-binding domain select a D(N/ D)XpY motif and bind to the Tyr292 negative regulatory phosphorylating site of ZAP-70. J Bio Chem 272:33140, 1997
    • (1997) J Bio Chem , vol.272 , pp. 33140
    • Lupher M.L., Jr.1    Songyang, Z.2    Shoelson, S.E.3    Cantley, L.C.4    Band, H.5
  • 63
    • 0032478805 scopus 로고
    • Fyn, Yes and Syk Phosphorylation sites in c-Cbl map to the same tyrosine residues that become phosphorylated in activated T cells
    • Feshchenko EA, Langdon WY, Tsygankov AY: Fyn, Yes and Syk Phosphorylation sites in c-Cbl map to the same tyrosine residues that become phosphorylated in activated T cells. J Biol Chem 273:8323, 1988
    • (1988) J Biol Chem , vol.273 , pp. 8323
    • Feshchenko, E.A.1    Langdon, W.Y.2    Tsygankov, A.Y.3
  • 65
    • 0029876948 scopus 로고    scopus 로고
    • Stimulation through the T-cell receptor induces Cbl association with Crk proteins and the guanine-nucleotide exchange protein C3G
    • Reedquist KAT, Panchamoorthy FG, Langdon WY, Shoelson SE, Druker BJ, Band H: Stimulation through the T-cell receptor induces Cbl association with Crk proteins and the guanine-nucleotide exchange protein C3G. J Biol Chem 271:8435, 1996
    • (1996) J Biol Chem , vol.271 , pp. 8435
    • Reedquist, K.A.T.1    Panchamoorthy, F.G.2    Langdon, W.Y.3    Shoelson, S.E.4    Druker, B.J.5    Band, H.6
  • 66
    • 0031394111 scopus 로고    scopus 로고
    • The Cbl family of signal transduction moleculs
    • Smit L, Borst J: The Cbl family of signal transduction moleculs. Crit Rev Oncol 8:359, 1997
    • (1997) Crit Rev Oncol , vol.8 , pp. 359
    • Smit, L.1    Borst, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.