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Volumn 34, Issue 2, 2006, Pages 143-155

Dual role of the adaptor protein SLP-65: Organizer of signal transduction and tumor suppressor of pre-B cell leukemia

Author keywords

B cell development; Btk; Leukemia; SLP 65; Tumor suppressor

Indexed keywords

ADAPTOR PROTEIN; B LYMPHOCYTE RECEPTOR; PROTEIN SLP65; UNCLASSIFIED DRUG;

EID: 33745683797     PISSN: 0257277X     EISSN: None     Source Type: Journal    
DOI: 10.1385/IR:34:2:143     Document Type: Review
Times cited : (4)

References (71)
  • 1
    • 0035575979 scopus 로고    scopus 로고
    • Surrogate light chain-mediated interaction of a soluble pre-B cell receptor with adherent cell lines
    • Bradl H, Jack HM: Surrogate light chain-mediated interaction of a soluble pre-B cell receptor with adherent cell lines. J Immunol 2001; 167 (11): 6403-6411.
    • (2001) J Immunol , vol.167 , Issue.11 , pp. 6403-6411
    • Bradl, H.1    Jack, H.M.2
  • 2
    • 0036790940 scopus 로고    scopus 로고
    • Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering
    • USA
    • Gauthier L, Rossi B, Roux F, Termine E, Schiff C: Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering. Proc Natl Acad Sci USA 2002; 99 (20): 13014-13019.
    • (2002) Proc Natl Acad Sci , vol.99 , Issue.20 , pp. 13014-13019
    • Gauthier, L.1    Rossi, B.2    Roux, F.3    Termine, E.4    Schiff, C.5
  • 3
    • 0029837933 scopus 로고    scopus 로고
    • Surrogate light chain in B cell development
    • Karasuyama H, Rolink A, Melchers F: Surrogate light chain in B cell development. Adv Immunol 1996; 63: 1-41.
    • (1996) Adv Immunol , vol.63 , pp. 1-41
    • Karasuyama, H.1    Rolink, A.2    Melchers, F.3
  • 4
    • 0025852445 scopus 로고
    • A B cell-deficient mouse by targeted disruption of the membrane exon of the immunoglobulin mu chain gene
    • Kitamura D, Roes J, Kuhn R, Rajewsky K: A B cell-deficient mouse by targeted disruption of the membrane exon of the immunoglobulin mu chain gene. Nature 1991; 350 (6317): 423-426.
    • (1991) Nature , vol.350 , Issue.6317 , pp. 423-426
    • Kitamura, D.1    Roes, J.2    Kuhn, R.3    Rajewsky, K.4
  • 5
    • 0034922992 scopus 로고    scopus 로고
    • IgA production without mu or delta chain expression in developing B cells
    • Macpherson AJ, Lamarre A, McCoy K, et al: IgA production without mu or delta chain expression in developing B cells. Nat Immunol 2001; 2 (7): 625-631.
    • (2001) Nat Immunol , vol.2 , Issue.7 , pp. 625-631
    • Macpherson, A.J.1    Lamarre, A.2    McCoy, K.3
  • 7
    • 18744437511 scopus 로고    scopus 로고
    • Partial block in B lymphocyte development at the transition into the pre-B cell receptor stage in Vpre-B1-deficient mice
    • Martensson A, Argon Y, Melchers F, Dul JL, Martensson IL: Partial block in B lymphocyte development at the transition into the pre-B cell receptor stage in Vpre-B1-deficient mice. Int Immunol 1999; 11 (3): 453-460.
    • (1999) Int Immunol , vol.11 , Issue.3 , pp. 453-460
    • Martensson, A.1    Argon, Y.2    Melchers, F.3    Dul, J.L.4    Martensson, I.L.5
  • 8
    • 0035910752 scopus 로고    scopus 로고
    • Loss of precursor B cell expansion but not allelic exclusion in VpreB1/VpreB2 double-deficient mice
    • Mundt C, Licence S, Shimizu T, Melchers F, Martensson IL: Loss of precursor B cell expansion but not allelic exclusion in VpreB1/VpreB2 double-deficient mice. J Exp Med 2001; 193 (4): 435-445.
    • (2001) J Exp Med , vol.193 , Issue.4 , pp. 435-445
    • Mundt, C.1    Licence, S.2    Shimizu, T.3    Melchers, F.4    Martensson, I.L.5
  • 9
    • 0029913115 scopus 로고    scopus 로고
    • Regulation of an early developmental checkpoint in the B cell pathway by Ig beta
    • Gong S, Nussenzweig MC: Regulation of an early developmental checkpoint in the B cell pathway by Ig beta. Science 1996; 272 (5260): 411-414.
    • (1996) Science , vol.272 , Issue.5260 , pp. 411-414
    • Gong, S.1    Nussenzweig, M.C.2
  • 10
    • 0037100435 scopus 로고    scopus 로고
    • B cell progenitors are arrested in maturation but have intact VDJ recombination in the absence of Ig-alpha and Ig-beta
    • Pelanda R, Braun U, Hobeika E, Nussenzweig MC, Reth M: B cell progenitors are arrested in maturation but have intact VDJ recombination in the absence of Ig-alpha and Ig-beta. J Immunol 2002; 169 (2): 865-872.
    • (2002) J Immunol , vol.169 , Issue.2 , pp. 865-872
    • Pelanda, R.1    Braun, U.2    Hobeika, E.3    Nussenzweig, M.C.4    Reth, M.5
  • 11
    • 0025068716 scopus 로고
    • Molecular components of the B-cell antigen receptor complex of the IgM class
    • Hombach J, Tsubata T, Leclercq L, Stappert H, Reth M: Molecular components of the B-cell antigen receptor complex of the IgM class. Nature 1990; 343 (6260): 760-762.
    • (1990) Nature , vol.343 , Issue.6260 , pp. 760-762
    • Hombach, J.1    Tsubata, T.2    Leclercq, L.3    Stappert, H.4    Reth, M.5
  • 12
    • 0028889302 scopus 로고
    • Perinatal lethality and blocked B-cell development in mice lacking the tyrosine kinase Syk
    • Turner M, Mee PJ, Costello PS, et al: Perinatal lethality and blocked B-cell development in mice lacking the tyrosine kinase Syk. Nature 1995; 378 (6554): 298-302.
    • (1995) Nature , vol.378 , Issue.6554 , pp. 298-302
    • Turner, M.1    Mee, P.J.2    Costello, P.S.3
  • 13
    • 0034646203 scopus 로고    scopus 로고
    • The B cell-restricted adaptor BASH is required for normal development and antigen receptor-mediated activation of B cells
    • USA
    • Hayashi K, Nittono R, Okamoto N, et al: The B cell-restricted adaptor BASH is required for normal development and antigen receptor-mediated activation of B cells. Proc Natl Acad Sci USA 2000; 97 (6): 2755-2760.
    • (2000) Proc Natl Acad Sci , vol.97 , Issue.6 , pp. 2755-2760
    • Hayashi, K.1    Nittono, R.2    Okamoto, N.3
  • 14
    • 0033229798 scopus 로고    scopus 로고
    • Abnormal development and function of B lymphocytes in mice deficient for the signaling adaptor protein SLP-65
    • Jumaa H, Wollscheid B, Mitterer M, Wienands J, Reth M, Nielsen PJ: Abnormal development and function of B lymphocytes in mice deficient for the signaling adaptor protein SLP-65. Immunity 1999; 11 (5): 547-554.
    • (1999) Immunity , vol.11 , Issue.5 , pp. 547-554
    • Jumaa, H.1    Wollscheid, B.2    Mitterer, M.3    Wienands, J.4    Reth, M.5    Nielsen, P.J.6
  • 15
    • 0028847329 scopus 로고
    • Defective B cell development and function in Btk-deficient mice
    • Khan WN, Alt FW, Gerstein RM, et al: Defective B cell development and function in Btk-deficient mice. Immunity 1995; 3 (3): 283-299.
    • (1995) Immunity , vol.3 , Issue.3 , pp. 283-299
    • Khan, W.N.1    Alt, F.W.2    Gerstein, R.M.3
  • 16
    • 0033521085 scopus 로고    scopus 로고
    • Requirement for B cell linker protein (BLNK) in B cell development
    • Pappu R, Cheng AM, Li B, et al: Requirement for B cell linker protein (BLNK) in B cell development. Science 1999; 286 (5446): 1949-1954.
    • (1999) Science , vol.286 , Issue.5446 , pp. 1949-1954
    • Pappu, R.1    Cheng, A.M.2    Li, B.3
  • 17
    • 0033624638 scopus 로고    scopus 로고
    • Phospholipase Cgamma2 is essential in the functions of B cell and several Fc receptors
    • Wang D, Feng J, Wen R, et al: Phospholipase Cgamma2 is essential in the functions of B cell and several Fc receptors. Immunity 2000; 13 (1): 25-35.
    • (2000) Immunity , vol.13 , Issue.1 , pp. 25-35
    • Wang, D.1    Feng, J.2    Wen, R.3
  • 18
    • 0034090263 scopus 로고    scopus 로고
    • B cell development and activation defects resulting in xid-like immunodeficiency in BLNK/SLP-65-deficient mice
    • Xu S, Tan JE, Wong EP, Manickam A, Ponniah S, Lam KP: B cell development and activation defects resulting in xid-like immunodeficiency in BLNK/SLP-65-deficient mice. Int Immunol 2000; 12 (3): 397-404.
    • (2000) Int Immunol , vol.12 , Issue.3 , pp. 397-404
    • Xu, S.1    Tan, J.E.2    Wong, E.P.3    Manickam, A.4    Ponniah, S.5    Lam, K.P.6
  • 19
    • 0033695960 scopus 로고    scopus 로고
    • Engagement of the human pre-B cell receptor generates a lipid raft-dependent calcium signaling complex
    • Guo B, Kato RM, Garcia-Lloret M, Wahl MI, Rawlings DJ: Engagement of the human pre-B cell receptor generates a lipid raft-dependent calcium signaling complex. Immunity 2000; 13 (2): 243-253.
    • (2000) Immunity , vol.13 , Issue.2 , pp. 243-253
    • Guo, B.1    Kato, R.M.2    Garcia-Lloret, M.3    Wahl, M.I.4    Rawlings, D.J.5
  • 20
    • 0034598353 scopus 로고    scopus 로고
    • Precursor B cell receptor-dependent B cell proliferation and differentiation does not require the bone marrow or fetal liver environment
    • Rolink AG, Winkler T, Melchers F, Andersson J: Precursor B cell receptor-dependent B cell proliferation and differentiation does not require the bone marrow or fetal liver environment. J Exp Med 2000; 191 (1): 23-32.
    • (2000) J Exp Med , vol.191 , Issue.1 , pp. 23-32
    • Rolink, A.G.1    Winkler, T.2    Melchers, F.3    Andersson, J.4
  • 21
    • 0035803539 scopus 로고    scopus 로고
    • Ligand-independent signaling functions for the B lymphocyte antigen receptor and their role in positive selection during B lymphopoiesis
    • Bannish G, Fuentes-Panana EM, Cambier JC, Pear WS, Monroe JG: Ligand-independent signaling functions for the B lymphocyte antigen receptor and their role in positive selection during B lymphopoiesis. J Exp Med 2001; 194 (11): 1583-1596.
    • (2001) J Exp Med , vol.194 , Issue.11 , pp. 1583-1596
    • Bannish, G.1    Fuentes-Panana, E.M.2    Cambier, J.C.3    Pear, W.S.4    Monroe, J.G.5
  • 22
    • 0033431772 scopus 로고    scopus 로고
    • A role for lipid rafts in B cell antigen receptor signaling and antigen targeting
    • Cheng PC, Dykstra ML, Mitchell RN, Pierce SK: A role for lipid rafts in B cell antigen receptor signaling and antigen targeting. J Exp Med 1999; 190 (11): 1549-1560.
    • (1999) J Exp Med , vol.190 , Issue.11 , pp. 1549-1560
    • Cheng, P.C.1    Dykstra, M.L.2    Mitchell, R.N.3    Pierce, S.K.4
  • 23
    • 0036866477 scopus 로고    scopus 로고
    • Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop
    • Rolli V, Gallwitz M, Wossning T, et al: Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop. Mol Cell 2002; 10 (5): 1057-1069.
    • (2002) Mol Cell , vol.10 , Issue.5 , pp. 1057-1069
    • Rolli, V.1    Gallwitz, M.2    Wossning, T.3
  • 24
    • 0032555744 scopus 로고    scopus 로고
    • Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide
    • Futterer K, Wong J, Grucza RA, Chan AC, Waksman G: Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide. J Mol Biol 1998; 281 (3): 523-537.
    • (1998) J Mol Biol , vol.281 , Issue.3 , pp. 523-537
    • Futterer, K.1    Wong, J.2    Grucza, R.A.3    Chan, A.C.4    Waksman, G.5
  • 25
    • 0028783396 scopus 로고
    • Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling
    • Kurosaki T, Johnson SA, Pao L, Sada K, Yamamura H, Cambier JC: Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling. J Exp Med 1995; 182 (6): 1815-1823.
    • (1995) J Exp Med , vol.182 , Issue.6 , pp. 1815-1823
    • Kurosaki, T.1    Johnson, S.A.2    Pao, L.3    Sada, K.4    Yamamura, H.5    Cambier, J.C.6
  • 26
    • 0037011114 scopus 로고    scopus 로고
    • BLNK: Molecular scaffolding through "cis"-mediated organization of signaling proteins
    • Chiu CW, Dalton M, Ishiai M, Kurosaki T, Chan AC: BLNK: molecular scaffolding through "cis"-mediated organization of signaling proteins. EMBO J 2002; 21 (23): 6461-6472.
    • (2002) EMBO J , vol.21 , Issue.23 , pp. 6461-6472
    • Chiu, C.W.1    Dalton, M.2    Ishiai, M.3    Kurosaki, T.4    Chan, A.C.5
  • 27
    • 0035956958 scopus 로고    scopus 로고
    • BLNK mediates Syk-dependent Btk activation
    • USA
    • Baba Y, Hashimoto S, Matsushita M, et al: BLNK mediates Syk-dependent Btk activation. Proc Nalt Acad Sci USA 2001; 98 (5): 2582-2586.
    • (2001) Proc Nalt Acad Sci , vol.98 , Issue.5 , pp. 2582-2586
    • Baba, Y.1    Hashimoto, S.2    Matsushita, M.3
  • 28
    • 0032055476 scopus 로고    scopus 로고
    • Btk/Tec kinases regulate sustained increases in intracellular Ca2+ following B-cell receptor activation
    • Fluckiger A-C, Li Z, Kato RM, et al: Btk/Tec kinases regulate sustained increases in intracellular Ca2+ following B-cell receptor activation. EMBO J 1998; 17 (7): 1973-1985.
    • (1998) EMBO J , vol.17 , Issue.7 , pp. 1973-1985
    • Fluckiger, A.-C.1    Li, Z.2    Kato, R.M.3
  • 29
    • 0032487507 scopus 로고    scopus 로고
    • Involvement of guanosine triphosphatases and phospholipase C-gamma2 in extracellular signal-regulated kinase, c-Jun NH2-terminal kinase, and p38 mitogen-activated protein kinase activation by the B cell antigen receptor
    • Hashimoto A, Okada H, Jiang A, et al: Involvement of guanosine triphosphatases and phospholipase C-gamma2 in extracellular signal-regulated kinase, c-Jun NH2-terminal kinase, and p38 mitogen-activated protein kinase activation by the B cell antigen receptor. J Exp Med 1998; 188 (7): 1287-1295.
    • (1998) J Exp Med , vol.188 , Issue.7 , pp. 1287-1295
    • Hashimoto, A.1    Okada, H.2    Jiang, A.3
  • 30
    • 0032487580 scopus 로고    scopus 로고
    • Different protein tyrosine kinases are required for B cell antigen receptor-mediated activation of extracellular signal-regulated kinase, c-Jun NH2-terminal kinase 1, and p38 mitogen-activated protein kinase
    • Jiang A, Craxton A, Kurosaki T, Clark EA: Different protein tyrosine kinases are required for B cell antigen receptor-mediated activation of extracellular signal-regulated kinase, c-Jun NH2-terminal kinase 1, and p38 mitogen-activated protein kinase. J Exp Med 1998; 188 (7): 1297-1306.
    • (1998) J Exp Med , vol.188 , Issue.7 , pp. 1297-1306
    • Jiang, A.1    Craxton, A.2    Kurosaki, T.3    Clark, E.A.4
  • 31
    • 0038094512 scopus 로고    scopus 로고
    • Regulation of Vav localization in membrane rafts by adaptor molecules Grb2 and BLNK
    • Johmura S, oh-hora M, Inabe K, et al: Regulation of Vav localization in membrane rafts by adaptor molecules Grb2 and BLNK. Immunity 2003; 18 (6): 777-787.
    • (2003) Immunity , vol.18 , Issue.6 , pp. 777-787
    • Johmura, S.1    Oh-hora, M.2    Inabe, K.3
  • 32
    • 0032541388 scopus 로고    scopus 로고
    • SLP-65: A new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation
    • Wienands J, Schweikert I, Wollscheid B, Jumaa H, Nielsen PJ, Reth M: SLP-65: a new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation. J Exp Med 1998; 188 (4): 791-795.
    • (1998) J Exp Med , vol.188 , Issue.4 , pp. 791-795
    • Wienands, J.1    Schweikert, I.2    Wollscheid, B.3    Jumaa, H.4    Nielsen, P.J.5    Reth, M.6
  • 33
    • 0029990003 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation
    • Rodriguez-Viciana P, Warne PH, Vanhaesebroeck B, Waterfield MD, Downward J: Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation. EMBO J 1996; 15 (10): 2442-2451.
    • (1996) EMBO J , vol.15 , Issue.10 , pp. 2442-2451
    • Rodriguez-Viciana, P.1    Warne, P.H.2    Vanhaesebroeck, B.3    Waterfield, M.D.4    Downward, J.5
  • 34
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek AB, Hollenberg SM, Cooper JA: Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 1993; 74 (1): 205-214.
    • (1993) Cell , vol.74 , Issue.1 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 35
    • 18244413206 scopus 로고    scopus 로고
    • Ras mediates effector pathways responsible for pre-B cell survival, which is essential for the developmental progression to the late pre-B cell stage
    • Nagaoka H, [???] et al: Ras mediates effector pathways responsible for pre-B cell survival, which is essential for the developmental progression to the late pre-B cell stage. J Exp Med 2000; 192 (2): 171-182.
    • (2000) J Exp Med , vol.192 , Issue.2 , pp. 171-182
    • Nagaoka, H.1
  • 36
    • 0033515093 scopus 로고    scopus 로고
    • Induction of Ig light chain gene rearrangement in heavy chain-deficient B cells by activated Ras
    • USA
    • Shaw AC, Swat W, Davidson L, Alt FW: Induction of Ig light chain gene rearrangement in heavy chain-deficient B cells by activated Ras. Proc Natl Acad Sci USA 1999; 96 (5): 2239-2243.
    • (1999) Proc Natl Acad Sci , vol.96 , Issue.5 , pp. 2239-2243
    • Shaw, A.C.1    Swat, W.2    Davidson, L.3    Alt, F.W.4
  • 37
    • 0033056366 scopus 로고    scopus 로고
    • BLNK required for coupling Syk to PLC gamma 2 and Rac1-JNK in B cells
    • Ishiai M, Kurosaki M, Pappu R, et al: BLNK required for coupling Syk to PLC gamma 2 and Rac1-JNK in B cells. Immunity 1999; 10 (1): 117-125.
    • (1999) Immunity , vol.10 , Issue.1 , pp. 117-125
    • Ishiai, M.1    Kurosaki, M.2    Pappu, R.3
  • 38
    • 0035827623 scopus 로고    scopus 로고
    • The adaptor protein BLNK is required for b cell antigen receptor-induced activation of nuclear factor-kappa B and cell cycle entry and survival of B lymphocytes
    • Tan JE, Wong SC, Gan SK, Xu S, Lam KP: The adaptor protein BLNK is required for b cell antigen receptor-induced activation of nuclear factor-kappa B and cell cycle entry and survival of B lymphocytes. J Biol Chem 2001; 276 (23): 20055-20063.
    • (2001) J Biol Chem , vol.276 , Issue.23 , pp. 20055-20063
    • Tan, J.E.1    Wong, S.C.2    Gan, S.K.3    Xu, S.4    Lam, K.P.5
  • 39
    • 0037234971 scopus 로고    scopus 로고
    • The adaptor protein SLP-65 acts as a tumor suppressor that limits pre-B cell expansion
    • Flemming A, Brummer T, Reth M, Jumaa H: The adaptor protein SLP-65 acts as a tumor suppressor that limits pre-B cell expansion. Nat Immunol 2003; 4 (1): 38-43.
    • (2003) Nat Immunol , vol.4 , Issue.1 , pp. 38-43
    • Flemming, A.1    Brummer, T.2    Reth, M.3    Jumaa, H.4
  • 40
    • 0026011211 scopus 로고
    • Long-term proliferating early pre B cell lines and clones with the potential to develop to surface Ig-positive, mitogen reactive B cells in vitro and in vivo
    • Rolink A, Kudo A, Karasuyama H, Kikuchi Y, Melchers F: Long-term proliferating early pre B cell lines and clones with the potential to develop to surface Ig-positive, mitogen reactive B cells in vitro and in vivo. EMBO J 1991; 10 (2): 327-336.
    • (1991) EMBO J , vol.10 , Issue.2 , pp. 327-336
    • Rolink, A.1    Kudo, A.2    Karasuyama, H.3    Kikuchi, Y.4    Melchers, F.5
  • 41
    • 0038526355 scopus 로고    scopus 로고
    • Deficiency of the adaptor SLP-65 in pre-B-cell acute lymphoblastic leukaemia
    • Jumaa H, Bossaller L, Portugal K, et al: Deficiency of the adaptor SLP-65 in pre-B-cell acute lymphoblastic leukaemia. Nature 2003; 423 (6938): 452-456.
    • (2003) Nature , vol.423 , Issue.6938 , pp. 452-456
    • Jumaa, H.1    Bossaller, L.2    Portugal, K.3
  • 42
    • 0035811561 scopus 로고    scopus 로고
    • Spleen tyrosine kinase (Syk) deficiency in childhood pro-B cell acute lymphoblastic leukemia
    • Goodman PA, Wood CM, Vassilev A, Mao C, Uckun FM: Spleen tyrosine kinase (Syk) deficiency in childhood pro-B cell acute lymphoblastic leukemia. Oncogene 2001; 20 (30): 3969-3978.
    • (2001) Oncogene , vol.20 , Issue.30 , pp. 3969-3978
    • Goodman, P.A.1    Wood, C.M.2    Vassilev, A.3    Mao, C.4    Uckun, F.M.5
  • 43
    • 0034932149 scopus 로고    scopus 로고
    • The absence of SLP65 and Btk blocks B cell development at the preB cell receptor-positive stage
    • Jumaa H, Mitterer M, Reth M, Nielsen PJ: The absence of SLP65 and Btk blocks B cell development at the preB cell receptor-positive stage. Eur J Immunol 2001; 31 (7): 2164-2169.
    • (2001) Eur J Immunol , vol.31 , Issue.7 , pp. 2164-2169
    • Jumaa, H.1    Mitterer, M.2    Reth, M.3    Nielsen, P.J.4
  • 44
    • 0037815206 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase cooperates with the B cell linker protein SLP-65 as a tumor suppressor in Pre-B cells
    • Kersseboom R, Middendorp S, Dingjan GM, et al: Bruton's tyrosine kinase cooperates with the B cell linker protein SLP-65 as a tumor suppressor in Pre-B cells. J Exp Med 2003; 198 (1): 91-98.
    • (2003) J Exp Med , vol.198 , Issue.1 , pp. 91-98
    • Kersseboom, R.1    Middendorp, S.2    Dingjan, G.M.3
  • 45
    • 0345447618 scopus 로고    scopus 로고
    • Function of Bruton's tyrosine kinase during B cell development is partially independent of its catalytic activity
    • Middendorp S, Dingjan GM, Maas A, Dahlenborg K, Hendriks RW: Function of Bruton's tyrosine kinase during B cell development is partially independent of its catalytic activity. J Immunol 2003; 171 (11): 5988-5996.
    • (2003) J Immunol , vol.171 , Issue.11 , pp. 5988-5996
    • Middendorp, S.1    Dingjan, G.M.2    Maas, A.3    Dahlenborg, K.4    Hendriks, R.W.5
  • 46
    • 0345138995 scopus 로고    scopus 로고
    • BTK regulates PtdIns-4,5-P2 synthesis: Importance for calcium signaling and PI3K activity
    • Saito K, Tolias KF, Saci A, et al: BTK regulates PtdIns-4,5-P2 synthesis: importance for calcium signaling and PI3K activity. Immunity 2003; 19 (5): 669-678.
    • (2003) Immunity , vol.19 , Issue.5 , pp. 669-678
    • Saito, K.1    Tolias, K.F.2    Saci, A.3
  • 47
    • 0032055484 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: A target for SHIP-mediated inhibitory signals
    • Scharenberg AM, El-Hillal O, Fruman DA, et al: Phosphatidylinositol-3,4, 5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals. EMBO J 1998; 17 (7): 1961-1972.
    • (1998) EMBO J , vol.17 , Issue.7 , pp. 1961-1972
    • Scharenberg, A.M.1    El-Hillal, O.2    Fruman, D.A.3
  • 48
    • 0033806860 scopus 로고    scopus 로고
    • Involvement of LAT, Gads, and Grb2 in compartmentation of SLP-76 to the plasma membrane
    • Ishiai M, Kurosaki M, Inabe K, Chan AC, Sugamura K, Kurosaki T: Involvement of LAT, Gads, and Grb2 in compartmentation of SLP-76 to the plasma membrane. J Exp Med 2000; 192 (6): 847-856.
    • (2000) J Exp Med , vol.192 , Issue.6 , pp. 847-856
    • Ishiai, M.1    Kurosaki, M.2    Inabe, K.3    Chan, A.C.4    Sugamura, K.5    Kurosaki, T.6
  • 49
    • 0041429608 scopus 로고    scopus 로고
    • LAT links the pre-BCR to calcium signaling
    • Su YW, Jumaa H: LAT links the pre-BCR to calcium signaling. Immunity 2003; 19 (2): 295-305.
    • (2003) Immunity , vol.19 , Issue.2 , pp. 295-305
    • Su, Y.W.1    Jumaa, H.2
  • 50
    • 0037121939 scopus 로고    scopus 로고
    • Non-T cell activation linker (NTAL): A transmembrane adaptor protein involved in immunoreceptor signaling
    • Brdicka T, Imrich M, Angelisova P, et al: Non-T cell activation linker (NTAL): a transmembrane adaptor protein involved in immunoreceptor signaling. J Exp Med 2002; 196 (12): 1617-1626.
    • (2002) J Exp Med , vol.196 , Issue.12 , pp. 1617-1626
    • Brdicka, T.1    Imrich, M.2    Angelisova, P.3
  • 51
    • 0037321012 scopus 로고    scopus 로고
    • LAB: A new membrane-associated adaptor molecule in B cell activation
    • Janssen E, Zhu M, Zhang W, Koonpaew S: LAB: a new membrane-associated adaptor molecule in B cell activation. Nat Immunol 2003; 4 (2): 117-123.
    • (2003) Nat Immunol , vol.4 , Issue.2 , pp. 117-123
    • Janssen, E.1    Zhu, M.2    Zhang, W.3    Koonpaew, S.4
  • 52
    • 0027262213 scopus 로고
    • Targets of B lymphocyte antigen receptor signal transduction include the p21ras GTPase-activating protein (GAP) and two GAP-associated proteins
    • Gold MR, Crowley MT, Martin GA, McCormick F, DeFranco AL: Targets of B lymphocyte antigen receptor signal transduction include the p21ras GTPase-activating protein (GAP) and two GAP-associated proteins. J Immunol 1993; 150 (2): 377-386.
    • (1993) J Immunol , vol.150 , Issue.2 , pp. 377-386
    • Gold, M.R.1    Crowley, M.T.2    Martin, G.A.3    McCormick, F.4    DeFranco, A.L.5
  • 53
    • 0025177324 scopus 로고
    • Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases
    • Ellis C, Moran M, McCormick F, Pawson T: Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature 1990; 343 (6256): 377-381.
    • (1990) Nature , vol.343 , Issue.6256 , pp. 377-381
    • Ellis, C.1    Moran, M.2    McCormick, F.3    Pawson, T.4
  • 54
    • 0035817343 scopus 로고    scopus 로고
    • p62(dok), a negative regulator of Ras and mitogen-activated protein kinase (MAPK) activity, opposes leukemogenesis by p210(bcr-abl)
    • Di Cristofano A, Niki M, Zhao M, et al: p62(dok), a negative regulator of Ras and mitogen-activated protein kinase (MAPK) activity, opposes leukemogenesis by p210(bcr-abl). J Exp Med 2001; 194 (3): 275-284.
    • (2001) J Exp Med , vol.194 , Issue.3 , pp. 275-284
    • Di Cristofano, A.1    Niki, M.2    Zhao, M.3
  • 55
    • 0034637559 scopus 로고    scopus 로고
    • Mediation by the protein-tyrosine kinase Tec of signaling between the B cell antigen receptor and Dok-1
    • Yoshida K, Yamashita Y, Miyazato A, et al: Mediation by the protein-tyrosine kinase Tec of signaling between the B cell antigen receptor and Dok-1. J Biol Chem 2000; 275 (32): 24945-24952.
    • (2000) J Biol Chem , vol.275 , Issue.32 , pp. 24945-24952
    • Yoshida, K.1    Yamashita, Y.2    Miyazato, A.3
  • 56
    • 0032006789 scopus 로고    scopus 로고
    • Expression and activation of the nonreceptor tyrosine kinase Tec in human B cells
    • Kitanaka A, Mano H, Conley ME, Campana D: Expression and activation of the nonreceptor tyrosine kinase Tec in human B cells. Blood 1998; 91 (3): 940-948.
    • (1998) Blood , vol.91 , Issue.3 , pp. 940-948
    • Kitanaka, A.1    Mano, H.2    Conley, M.E.3    Campana, D.4
  • 57
    • 0842346437 scopus 로고    scopus 로고
    • Principles of tumor suppression
    • Sherr CJ: Principles of tumor suppression. Cell 2004; 116 (2): 235-246.
    • (2004) Cell , vol.116 , Issue.2 , pp. 235-246
    • Sherr, C.J.1
  • 58
    • 0036798665 scopus 로고    scopus 로고
    • Control of pre-BCR signaling by Pax5-dependent activation of the BLNK gene
    • Schebesta M, Pfeffer PL, Busslinger M: Control of pre-BCR signaling by Pax5-dependent activation of the BLNK gene. Immunity 2002; 17 (4): 473-485.
    • (2002) Immunity , vol.17 , Issue.4 , pp. 473-485
    • Schebesta, M.1    Pfeffer, P.L.2    Busslinger, M.3
  • 59
    • 0030010591 scopus 로고    scopus 로고
    • Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors
    • Nakayama K, Ishida N, Shirane M, et al: Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors. Cell 1996; 85 (5): 707-720.
    • (1996) Cell , vol.85 , Issue.5 , pp. 707-720
    • Nakayama, K.1    Ishida, N.2    Shirane, M.3
  • 60
    • 0030498092 scopus 로고    scopus 로고
    • A conserved degradation signal regulates RAG-2 accumulation during cell division and links V(D)J recombination to the cell cycle
    • Li Z, Dordai DI, Lee J, Desiderio S: A conserved degradation signal regulates RAG-2 accumulation during cell division and links V(D)J recombination to the cell cycle. Immunity 1996; 5 (6): 575-589.
    • (1996) Immunity , vol.5 , Issue.6 , pp. 575-589
    • Li, Z.1    Dordai, D.I.2    Lee, J.3    Desiderio, S.4
  • 61
    • 0028223271 scopus 로고
    • Cell cycle regulation of V(D)J recombination-activating protein RAG-2
    • USA
    • Lin WC, Desiderio S: Cell cycle regulation of V(D)J recombination- activating protein RAG-2. Proc Natl Acad Sci USA 1994; 91 (7): 2733-2737.
    • (1994) Proc Natl Acad Sci , vol.91 , Issue.7 , pp. 2733-2737
    • Lin, W.C.1    Desiderio, S.2
  • 62
    • 0036829568 scopus 로고    scopus 로고
    • RAG2 is down-regulated by cytoplasmic sequestration and ubiquitin-dependent degradation
    • Mizuta R, Mizuta M, Araki S, Kitamura D: RAG2 is down-regulated by cytoplasmic sequestration and ubiquitin-dependent degradation. J Biol Chem 2002; 277 (44): 41,423-41,427.
    • (2002) J Biol Chem , vol.277 , Issue.44
    • Mizuta, R.1    Mizuta, M.2    Araki, S.3    Kitamura, D.4
  • 63
    • 0033427205 scopus 로고    scopus 로고
    • Cyclin A/CDK2 regulates V(D)J recombination by coordinating RAG-2 accumulation and DNA repair
    • Lee J, Desiderio S: Cyclin A/CDK2 regulates V(D)J recombination by coordinating RAG-2 accumulation and DNA repair. Immunity 1999; 11 (6): 771-781.
    • (1999) Immunity , vol.11 , Issue.6 , pp. 771-781
    • Lee, J.1    Desiderio, S.2
  • 64
    • 0033553390 scopus 로고    scopus 로고
    • Down-regulation of p27(Kip1) by two mechanisms, ubiquitin-mediated degradation and proteolytic processing
    • Shirane M, Harumiya Y, Ishida N, et al: Down-regulation of p27(Kip1) by two mechanisms, ubiquitin-mediated degradation and proteolytic processing. J Biol Chem 1999; 274 (20): 13,886-13,893.
    • (1999) J Biol Chem , vol.274 , Issue.20
    • Shirane, M.1    Harumiya, Y.2    Ishida, N.3
  • 65
    • 0035921821 scopus 로고    scopus 로고
    • A mouse knock-in model exposes sequential proteolytic pathways that regulate p27Kip1 in G1 and S phase
    • Malek NP, Sundberg H, McGrew S, Nakayama K, Kyriakides TR, Roberts JM: A mouse knock-in model exposes sequential proteolytic pathways that regulate p27Kip1 in G1 and S phase. Nature 2001; 413 (6853): 323-327.
    • (2001) Nature , vol.413 , Issue.6853 , pp. 323-327
    • Malek, N.P.1    Sundberg, H.2    McGrew, S.3    Nakayama, K.4    Kyriakides, T.R.5    Roberts, J.M.6
  • 66
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • Pagano M, [???]Tam SW, Theodoras AM, et al: Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 1995; 269 (5224): 682-685.
    • (1995) Science , vol.269 , Issue.5224 , pp. 682-685
    • Pagano, M.1    Tam, S.W.2    Theodoras, A.M.3
  • 67
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano AC, Eytan E, Hershko A, Pagano M: SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat Cell Biol 1999; 1 (4): 193-199.
    • (1999) Nat Cell Biol , vol.1 , Issue.4 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 68
    • 0033174070 scopus 로고    scopus 로고
    • p45SKP2 promotes p27Kip1 degradation and induces S phase in quiescent cells
    • Sutterluty H, Chatelain E, Marti A, et al: p45SKP2 promotes p27Kip1 degradation and induces S phase in quiescent cells. Nat Cell Biol 1999; 1 (4): 207-214.
    • (1999) Nat Cell Biol , vol.1 , Issue.4 , pp. 207-214
    • Sutterluty, H.1    Chatelain, E.2    Marti, A.3
  • 69
    • 0033578073 scopus 로고    scopus 로고
    • p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
    • Tsvetkov LM, Yeh KH, Lee SJ, Sun H, Zhang H: p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27. Curr Biol 1999; 9 (12): 661-664.
    • (1999) Curr Biol , vol.9 , Issue.12 , pp. 661-664
    • Tsvetkov, L.M.1    Yeh, K.H.2    Lee, S.J.3    Sun, H.4    Zhang, H.5
  • 70
    • 20444403003 scopus 로고    scopus 로고
    • Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle
    • Jiang H, Chang FC, Ross AE, Lee J, Nakayama K, Desiderio S: Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle. Mol Cell 2005; 18 (6): 699-709.
    • (2005) Mol Cell , vol.18 , Issue.6 , pp. 699-709
    • Jiang, H.1    Chang, F.C.2    Ross, A.E.3    Lee, J.4    Nakayama, K.5    Desiderio, S.6
  • 71
    • 1442284076 scopus 로고    scopus 로고
    • Negative regulation of SCFSkp2 ubiquitin ligase by TGF-beta signaling
    • Wang W, Ungermannova D, Jin J, Harper JW, Liu X: Negative regulation of SCFSkp2 ubiquitin ligase by TGF-beta signaling. Oncogene 2004; 23 (5): 1064-1075.
    • (2004) Oncogene , vol.23 , Issue.5 , pp. 1064-1075
    • Wang, W.1    Ungermannova, D.2    Jin, J.3    Harper, J.W.4    Liu, X.5


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