-
1
-
-
0028014460
-
Signal transduction by lymphocyte antigen receptors
-
Weiss A, Littman DR. Signal transduction by lymphocyte antigen receptors. Cell. 76:1994;263-274.
-
(1994)
Cell
, vol.76
, pp. 263-274
-
-
Weiss, A.1
Littman, D.R.2
-
2
-
-
0030831199
-
The complexity of signaling pathways activated by the BCR
-
DeFranco AL. The complexity of signaling pathways activated by the BCR. Curr Opin Immunol. 9:1997;296-308.
-
(1997)
Curr Opin Immunol
, vol.9
, pp. 296-308
-
-
Defranco, A.L.1
-
3
-
-
0025285280
-
Increases in tyrosine phosphorylation are detectable before phospholipase C activation after T cell receptor stimulation
-
June CH, Fletcher MC, Ledbetter JA, Samelson LE. Increases in tyrosine phosphorylation are detectable before phospholipase C activation after T cell receptor stimulation. J Immunol. 144:1990;1591-1599.
-
(1990)
J Immunol
, vol.144
, pp. 1591-1599
-
-
June, C.H.1
Fletcher, M.C.2
Ledbetter, J.A.3
Samelson, L.E.4
-
4
-
-
0026705903
-
Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor
-
Straus DB, Weiss A. Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell. 70:1992;585-593.
-
(1992)
Cell
, vol.70
, pp. 585-593
-
-
Straus, D.B.1
Weiss, A.2
-
5
-
-
0028355565
-
Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling
-
Kurosaki T, Takata M, Yamanashi Y, Inazu T, Taniguchi T, Yamamoto T, Yamamura H. Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling. J Exp Med. 179:1994;1725-1729.
-
(1994)
J Exp Med
, vol.179
, pp. 1725-1729
-
-
Kurosaki, T.1
Takata, M.2
Yamanashi, Y.3
Inazu, T.4
Taniguchi, T.5
Yamamoto, T.6
Yamamura, H.7
-
6
-
-
0026095639
-
Functional activation of the T-cell antigen receptor induces tyrosine phosphorylation of phospholipase C-gamma 1
-
Weiss A, Koretzky G, Schatzman RC, Kadlecek T. Functional activation of the T-cell antigen receptor induces tyrosine phosphorylation of phospholipase C-gamma 1. Proc Natl Acad Sci USA. 88:1991;5484-5488.
-
(1991)
Proc Natl Acad Sci USA
, vol.88
, pp. 5484-5488
-
-
Weiss, A.1
Koretzky, G.2
Schatzman, R.C.3
Kadlecek, T.4
-
7
-
-
0026577239
-
Tyrosine phosphorylation of phospholipase C-gamma 2 upon cross-linking of membrane Ig on murine B lymphocytes
-
Hempel WM, Schatzman RC, DeFranco AL. Tyrosine phosphorylation of phospholipase C-gamma 2 upon cross-linking of membrane Ig on murine B lymphocytes. J Immunol. 148:1992;3021-3027.
-
(1992)
J Immunol
, vol.148
, pp. 3021-3027
-
-
Hempel, W.M.1
Schatzman, R.C.2
Defranco, A.L.3
-
8
-
-
0026483786
-
ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR zeta chain
-
Chan AC, Iwashima M, Turck CW, Weiss A. ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain. Cell. 71:1992;649-662.
-
(1992)
Cell
, vol.71
, pp. 649-662
-
-
Chan, A.C.1
Iwashima, M.2
Turck, C.W.3
Weiss, A.4
-
9
-
-
0028321540
-
Molecular cloning of human Syk A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex
-
Law CL, Sidorenko SP, Chandran KA, Draves KE, Chan AC, Weiss A, Edelhoff S, Disteche CM, Clark EA. Molecular cloning of human Syk A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex. J Biol Chem. 269:1994;12310-12319.
-
(1994)
J Biol Chem
, vol.269
, pp. 12310-12319
-
-
Law, C.L.1
Sidorenko, S.P.2
Chandran, K.A.3
Draves, K.E.4
Chan, A.C.5
Weiss, A.6
Edelhoff, S.7
Disteche, C.M.8
Clark, E.A.9
-
10
-
-
0031457622
-
Signaling through scaffold, anchoring, and adaptor proteins
-
of outstanding interest. This review discusses structural features of adaptor proteins in lymphocytes and other cells which allow specificity in the recruitment of signaling molecules to mediate diverse cellular responses.
-
Pawson T, Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. of outstanding interest Science. 278:1997;2075-2080 This review discusses structural features of adaptor proteins in lymphocytes and other cells which allow specificity in the recruitment of signaling molecules to mediate diverse cellular responses.
-
(1997)
Science
, vol.278
, pp. 2075-2080
-
-
Pawson, T.1
Scott, J.D.2
-
11
-
-
0027977799
-
SH2/SH3 signaling proteins
-
Schlessinger J. SH2/SH3 signaling proteins. Curr Opin Genet Dev. 4:1994;25-30.
-
(1994)
Curr Opin Genet Dev
, vol.4
, pp. 25-30
-
-
Schlessinger, J.1
-
12
-
-
0028596158
-
An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
-
Kavanaugh WM, Williams LT. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science. 266:1994;1862-1865.
-
(1994)
Science
, vol.266
, pp. 1862-1865
-
-
Kavanaugh, W.M.1
Williams, L.T.2
-
13
-
-
0028021882
-
Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
-
Harlan JE, Hajduk PJ, Yoon HS, Fesik SW. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature. 371:1994;168-170.
-
(1994)
Nature
, vol.371
, pp. 168-170
-
-
Harlan, J.E.1
Hajduk, P.J.2
Yoon, H.S.3
Fesik, S.W.4
-
14
-
-
0029146950
-
Characterization of a novel protein-binding module - The WW domain
-
Sudol M, Chen HI, Bougeret C, Einbond A, Bork P. Characterization of a novel protein-binding module - the WW domain. FEBS Lett. 369:1995;67-71.
-
(1995)
FEBS Lett
, vol.369
, pp. 67-71
-
-
Sudol, M.1
Chen, H.I.2
Bougeret, C.3
Einbond, A.4
Bork, P.5
-
15
-
-
0030293766
-
Protein - Protein interactions: PDZ domain networks
-
Fanning AS, Anderson JM. Protein - protein interactions: PDZ domain networks. Curr Biol. 6:1996;1385-1388.
-
(1996)
Curr Biol
, vol.6
, pp. 1385-1388
-
-
Fanning, A.S.1
Anderson, J.M.2
-
16
-
-
0026729382
-
The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
-
Lowenstein EJ, Daly RJ, Batzer AG, Li W, Margolis B, Lammers R, Ullrich A, Skolnik EY, Bar-Sagi D, Schlessinger J. The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell. 70:1992;431-442.
-
(1992)
Cell
, vol.70
, pp. 431-442
-
-
Lowenstein, E.J.1
Daly, R.J.2
Batzer, A.G.3
Li, W.4
Margolis, B.5
Lammers, R.6
Ullrich, A.7
Skolnik, E.Y.8
Bar-Sagi, D.9
Schlessinger, J.10
-
17
-
-
0027153103
-
Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adaptor protein, and Sos nucleotide exchange factor
-
Buday L, Downward J. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adaptor protein, and Sos nucleotide exchange factor. Cell. 73:1993;611-620.
-
(1993)
Cell
, vol.73
, pp. 611-620
-
-
Buday, L.1
Downward, J.2
-
18
-
-
0027910431
-
Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
-
Egan SE, Giddings BW, Brooks MW, Buday L, Sizeland AM, Weinberg RA. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature. 363:1993;45-51.
-
(1993)
Nature
, vol.363
, pp. 45-51
-
-
Egan, S.E.1
Giddings, B.W.2
Brooks, M.W.3
Buday, L.4
Sizeland, A.M.5
Weinberg, R.A.6
-
19
-
-
0030002817
-
Characterization of the roles of SH2 domain-containing proteins in T-lymphocyte activation by using dominant negative SH2 domains
-
of special interest. This study examines the roles of Src homology-2 (SH2) domains in TCR signaling. Through studies conducted in T cells overexpressing isolated SH2 domains from Grb2 or Shc, the authors conclude that Grb2, but not Shc, is critical for TCR signaling.
-
Northrop JP, Pustelnik MJ, Lu AT, Grove JR. Characterization of the roles of SH2 domain-containing proteins in T-lymphocyte activation by using dominant negative SH2 domains. of special interest Mol Cell Biol. 16:1996;2255-2263 This study examines the roles of Src homology-2 (SH2) domains in TCR signaling. Through studies conducted in T cells overexpressing isolated SH2 domains from Grb2 or Shc, the authors conclude that Grb2, but not Shc, is critical for TCR signaling.
-
(1996)
Mol Cell Biol
, vol.16
, pp. 2255-2263
-
-
Northrop, J.P.1
Pustelnik, M.J.2
Lu, A.T.3
Grove, J.R.4
-
20
-
-
0028227284
-
SH3 domains of the adaptor molecule Grb2 complex with two proteins in T cells: The guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases
-
Reif K, Buday L, Downward J, Cantrell DA. SH3 domains of the adaptor molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases. J Biol Chem. 269:1994;14081-14087.
-
(1994)
J Biol Chem
, vol.269
, pp. 14081-14087
-
-
Reif, K.1
Buday, L.2
Downward, J.3
Cantrell, D.A.4
-
21
-
-
0028245832
-
A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells
-
Buday L, Egan SE, Rodriguez Viciana P, Cantrell DA, Downward J. A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells. J Biol Chem. 269:1994;9019-9023.
-
(1994)
J Biol Chem
, vol.269
, pp. 9019-9023
-
-
Buday, L.1
Egan, S.E.2
Rodriguez Viciana, P.3
Cantrell, D.A.4
Downward, J.5
-
23
-
-
0028829346
-
Negative feedback regulation and desensitization of insulin- And epidermal growth factor-stimulated p21ras activation
-
Langlois WJ, Sasacka T, Saltiel AR, Olefsky JM. Negative feedback regulation and desensitization of insulin- and epidermal growth factor-stimulated p21ras activation. J Biol Chem. 270:1995;25320-25323.
-
(1995)
J Biol Chem
, vol.270
, pp. 25320-25323
-
-
Langlois, W.J.1
Sasacka, T.2
Saltiel, A.R.3
Olefsky, J.M.4
-
24
-
-
0028950637
-
Insulin-stimulated disassociation of the SOS-Grb2 complex
-
Waters SB, Yamauchi K, Pessin JE. Insulin-stimulated disassociation of the SOS-Grb2 complex. Mol Cell Biol. 15:1995;2791-2799.
-
(1995)
Mol Cell Biol
, vol.15
, pp. 2791-2799
-
-
Waters, S.B.1
Yamauchi, K.2
Pessin, J.E.3
-
25
-
-
0030764963
-
T cell receptor-induced phosphorylation of Sos requires activity of CD45, Lck, and protein kinase C, but not ERK
-
Zhao H, Li YY, Fucini RV, Ross SE, Pessin JE, Koretzky GA. T cell receptor-induced phosphorylation of Sos requires activity of CD45, Lck, and protein kinase C, but not ERK. J Biol Chem. 272:1997;21625-21634.
-
(1997)
J Biol Chem
, vol.272
, pp. 21625-21634
-
-
Zhao, H.1
Li, Y.Y.2
Fucini, R.V.3
Ross, S.E.4
Pessin, J.E.5
Koretzky, G.A.6
-
26
-
-
0026777369
-
A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction
-
Pellicci G, Lanfrancone L, Grignani F, McGlade J, Cavallo F, Forni G, Nicoletti I, Grignani F, Pawson T, Pelicci PG. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell. 70:1992;93-104.
-
(1992)
Cell
, vol.70
, pp. 93-104
-
-
Pellicci, G.1
Lanfrancone, L.2
Grignani, F.3
McGlade, J.4
Cavallo, F.5
Forni, G.6
Nicoletti, I.7
Grignani, F.8
Pawson, T.9
Pelicci, P.G.10
-
27
-
-
0028568639
-
A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors
-
Blaikie P, Immanuel D, Wu J, Li N, Yajnik V, Margolis B. A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J Biol Chem. 269:1994;32031-32034.
-
(1994)
J Biol Chem
, vol.269
, pp. 32031-32034
-
-
Blaikie, P.1
Immanuel, D.2
Wu, J.3
Li, N.4
Yajnik, V.5
Margolis, B.6
-
28
-
-
0027724634
-
Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation
-
Ravichandran KS, Lee KK, Songyang Z, Cantley LC, Bum P, Burakoff SJ. Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation. Science. 262:1993;902-905.
-
(1993)
Science
, vol.262
, pp. 902-905
-
-
Ravichandran, K.S.1
Lee, K.K.2
Songyang, Z.3
Cantley, L.C.4
Bum, P.5
Burakoff, S.J.6
-
29
-
-
0029072239
-
A comparison of the interaction of Shc and the tyrosine kinase ZAP-70 with the T cell antigen receptor zeta chain tyrosine-based activation motif
-
Osman N, Lucas SC, Turner H, Cantrell D. A comparison of the interaction of Shc and the tyrosine kinase ZAP-70 with the T cell antigen receptor zeta chain tyrosine-based activation motif. J Biol Chem. 270:1995;13981-13986.
-
(1995)
J Biol Chem
, vol.270
, pp. 13981-13986
-
-
Osman, N.1
Lucas, S.C.2
Turner, H.3
Cantrell, D.4
-
30
-
-
0028901649
-
Tyrosine phosphorylation of Shc is mediated through Lyn and Syk in B cell receptor signaling
-
Nagai K, Takata M, Yamamura H, Kurosaki T. Tyrosine phosphorylation of Shc is mediated through Lyn and Syk in B cell receptor signaling. J Biol Chem. 270:1995;6824-6829.
-
(1995)
J Biol Chem
, vol.270
, pp. 6824-6829
-
-
Nagai, K.1
Takata, M.2
Yamamura, H.3
Kurosaki, T.4
-
31
-
-
0030962699
-
Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes
-
of special interest. This study presents evidence that B-cell receptor-induced tyrosine phosphorylation of Shc results in Shc/Grb2 association, and that two tyrosine residues on Shc are required for the Grb2/Shc binding. The authors propose that the Shc/Grb2 complex provides a model mechanism for stabilization of Grb2/Sos association.
-
Harmer SL, DeFranco AL. Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes. of special interest Mol Cell Biol. 17:1997;4087-4095 This study presents evidence that B-cell receptor-induced tyrosine phosphorylation of Shc results in Shc/Grb2 association, and that two tyrosine residues on Shc are required for the Grb2/Shc binding. The authors propose that the Shc/Grb2 complex provides a model mechanism for stabilization of Grb2/Sos association.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 4087-4095
-
-
Harmer, S.L.1
Defranco, A.L.2
-
32
-
-
0029831323
-
Formation of Shc/Grb2- And Crk adaptor complexes containing tyrosine phosphorylated Cbl upon stimulation of the B-cell antigen receptor
-
Smit L, van der Horst G, Borst J. Formation of Shc/Grb2- and Crk adaptor complexes containing tyrosine phosphorylated Cbl upon stimulation of the B-cell antigen receptor. Oncogene. 13:1996;381-389.
-
(1996)
Oncogene
, vol.13
, pp. 381-389
-
-
Smit, L.1
Van Der Horst, G.2
Borst, J.3
-
33
-
-
0030610802
-
Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP
-
of special interest. This paper describes studies with 5′-inositol phosphatase (SHIP) point mutants which identify two tyrosine residues important for binding the Shc adaptor protein. The Shc/SHIP complex may function to inhibit TCR signaling.
-
Lamkin TD, Walk SF, Liu L, Damen JE, Krystal G, Ravichandran KS. Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP. of special interest J Biol Chem. 272:1997;10396-10401 This paper describes studies with 5′-inositol phosphatase (SHIP) point mutants which identify two tyrosine residues important for binding the Shc adaptor protein. The Shc/SHIP complex may function to inhibit TCR signaling.
-
(1997)
J Biol Chem
, vol.272
, pp. 10396-10401
-
-
Lamkin, T.D.1
Walk, S.F.2
Liu, L.3
Damen, J.E.4
Krystal, G.5
Ravichandran, K.S.6
-
34
-
-
0030587116
-
Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP
-
Chacko GW, Tridandapani S, Damen JE, Liu L, Krystal G, Coggeshall KM. Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP. J Immunol. 157:1996;2234-2238.
-
(1996)
J Immunol
, vol.157
, pp. 2234-2238
-
-
Chacko, G.W.1
Tridandapani, S.2
Damen, J.E.3
Liu, L.4
Krystal, G.5
Coggeshall, K.M.6
-
35
-
-
0031065146
-
Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions
-
of special interest. This work provides evidence that negative signaling via the IgG receptor FcγRII in B cells correlates with dissociation of Shc/Grb2, association between Shc and the phosphatase SHIP, and blunted Ras activation.
-
Tridandapani S, Chacko GW, Van Brocklyn JR, Coggeshall KM. Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions. of special interest J Immunol. 158:1997;1125-1132 This work provides evidence that negative signaling via the IgG receptor FcγRII in B cells correlates with dissociation of Shc/Grb2, association between Shc and the phosphatase SHIP, and blunted Ras activation.
-
(1997)
J Immunol
, vol.158
, pp. 1125-1132
-
-
Tridandapani, S.1
Chacko, G.W.2
Van Brocklyn, J.R.3
Coggeshall, K.M.4
-
36
-
-
0028928422
-
Molecular cloning of SLP-76, a 76kDa tyrosine phosphoprotein associated with Grb2 in T cells
-
Jackman J, Motto D, Sun O, Tanemoto M, Turck C, Peltz G, Koretzky G, Findell P. Molecular cloning of SLP-76, a 76kDa tyrosine phosphoprotein associated with Grb2 in T cells. J Biol Chem. 270:1995;7029-7032.
-
(1995)
J Biol Chem
, vol.270
, pp. 7029-7032
-
-
Jackman, J.1
Motto, D.2
Sun, O.3
Tanemoto, M.4
Turck, C.5
Peltz, G.6
Koretzky, G.7
Findell, P.8
-
37
-
-
0030002904
-
Implication of the GRB2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production
-
of outstanding interest. A demonstration that SLP-76 overexpression in Jurkat T cells dramatically augments TCR-stimulated nuclear factor of activated T cells (NFAT) and IL-2 gene activity.
-
Motto DG, Ross SE, Wu J, Hendricks-Taylor LR, Koretzky GA. Implication of the GRB2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production. of outstanding interest J Exp Med. 183:1996;1937-1943 A demonstration that SLP-76 overexpression in Jurkat T cells dramatically augments TCR-stimulated nuclear factor of activated T cells (NFAT) and IL-2 gene activity.
-
(1996)
J Exp Med
, vol.183
, pp. 1937-1943
-
-
Motto, D.G.1
Ross, S.E.2
Wu, J.3
Hendricks-Taylor, L.R.4
Koretzky, G.A.5
-
38
-
-
0031021586
-
SLP-76 is a substrate for the high affinity IgE receptor stimulated protein tyrosine kinases in rat basophilic leukemia cells
-
Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA. SLP-76 is a substrate for the high affinity IgE receptor stimulated protein tyrosine kinases in rat basophilic leukemia cells. J Biol Chem. 272:1996;1363-1367.
-
(1996)
J Biol Chem
, vol.272
, pp. 1363-1367
-
-
Hendricks-Taylor, L.R.1
Motto, D.G.2
Zhang, J.3
Siraganian, R.P.4
Koretzky, G.A.5
-
39
-
-
0030611753
-
The Ig alpha/Ig beta heterodimer on mu-negative proB cells is competent for transducing signals to induce early B cell differentiation
-
Nagata K, Nakamura T, Kitamura F, Kuramochi S, Taki S, Campbell KS, Karasuyama H. The Ig alpha/Ig beta heterodimer on mu-negative proB cells is competent for transducing signals to induce early B cell differentiation. Immunity. 7:1997;559-570.
-
(1997)
Immunity
, vol.7
, pp. 559-570
-
-
Nagata, K.1
Nakamura, T.2
Kitamura, F.3
Kuramochi, S.4
Taki, S.5
Campbell, K.S.6
Karasuyama, H.7
-
40
-
-
0029829894
-
Hematopoietic cell phosphatase, SHP-1, is constitutively associated with the SH2 domain-containing leukocyte protein, SLP-76, in B cells
-
Mizuno K, Katagiri T, Hasegawa K, Ogimoto M, Yakura H. Hematopoietic cell phosphatase, SHP-1, is constitutively associated with the SH2 domain-containing leukocyte protein, SLP-76, in B cells. J Exp Med. 184:1996;457-464.
-
(1996)
J Exp Med
, vol.184
, pp. 457-464
-
-
Mizuno, K.1
Katagiri, T.2
Hasegawa, K.3
Ogimoto, M.4
Yakura, H.5
-
41
-
-
0030869427
-
Identification of two tyrosine phosphoproteins, pp70 and pp68, which interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen receptor activation
-
Fu C, Chan AC. Identification of two tyrosine phosphoproteins, pp70 and pp68, which interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen receptor activation. J Biol Chem. 272:1997;27362-27368.
-
(1997)
J Biol Chem
, vol.272
, pp. 27362-27368
-
-
Fu, C.1
Chan, A.C.2
-
42
-
-
0031571263
-
Three domains of SLP-76 are required for its optimal function in a T cell line
-
of outstanding interest. These experiments demonstrate that the Src homology-2 (SH2) domain-containing phosphoprotein SLP-76 function in augmenting TCR-stimulated nuclear factor of activated T cells (NFAT) activation depends both upon TCR-mediated activation of tyrosine kinases and upon the presence of all three functional SLP-76 domains: the SH2 domain, the Grb2-binding site, and amino-terminal phosphorylated tyrosine residues. SLP-76 augmentation of TCR-induced AP1 activity is also shown.
-
Musci MA, Motto DG, Ross SE, Fang N, Koretzky GA. Three domains of SLP-76 are required for its optimal function in a T cell line. of outstanding interest J Immunol. 159:1997;1639-1647 These experiments demonstrate that the Src homology-2 (SH2) domain-containing phosphoprotein SLP-76 function in augmenting TCR-stimulated nuclear factor of activated T cells (NFAT) activation depends both upon TCR-mediated activation of tyrosine kinases and upon the presence of all three functional SLP-76 domains: the SH2 domain, the Grb2-binding site, and amino-terminal phosphorylated tyrosine residues. SLP-76 augmentation of TCR-induced AP1 activity is also shown.
-
(1997)
J Immunol
, vol.159
, pp. 1639-1647
-
-
Musci, M.A.1
Motto, D.G.2
Ross, S.E.3
Fang, N.4
Koretzky, G.A.5
-
43
-
-
0000082758
-
Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function
-
of special interest. Both this paper and Fang et al. [44] use point mutagenesis to demonstrate that inducible tyrosine phosphorylation is required for the ability of the phosphoprotein SLP-76 to augment TCR-stimulated activation of the nuclear factor of activated T cells. Additional evidence is provided in Wardenburg et al. for the likelihood that SLP-76 serves as an in vivo substrate of ZAP-70.
-
Wardenburg JB, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR. Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function. of special interest J Biol Chem. 271:1996;19641-19644 Both this paper and Fang et al. [44] use point mutagenesis to demonstrate that inducible tyrosine phosphorylation is required for the ability of the phosphoprotein SLP-76 to augment TCR-stimulated activation of the nuclear factor of activated T cells. Additional evidence is provided in Wardenburg et al. for the likelihood that SLP-76 serves as an in vivo substrate of ZAP-70.
-
(1996)
J Biol Chem
, vol.271
, pp. 19641-19644
-
-
Wardenburg, J.B.1
Fu, C.2
Jackman, J.K.3
Flotow, H.4
Wilkinson, S.E.5
Williams, D.H.6
Johnson, R.7
Kong, G.8
Chan, A.C.9
Findell, P.R.10
-
44
-
-
0030293529
-
Tyrosines 113, 128, and 145 of SLP-76 are required for optimal augmentation of NFAT promoter activity
-
of special interest. Both this paper and Wardenburg et al. [43] use point mutagenesis to demonstrate that inducible tyrosine phosphorylation is required for the ability of the phosphoprotein SLP-76 to augment TCR-stimulated activation of the nuclear factor of activated T cells (NFAT).
-
Fang N, Motto DG, Ross SE, Koretzky GA. Tyrosines 113, 128, and 145 of SLP-76 are required for optimal augmentation of NFAT promoter activity. of special interest J Immunol. 157:1996;3769-3773 Both this paper and Wardenburg et al. [43] use point mutagenesis to demonstrate that inducible tyrosine phosphorylation is required for the ability of the phosphoprotein SLP-76 to augment TCR-stimulated activation of the nuclear factor of activated T cells (NFAT).
-
(1996)
J Immunol
, vol.157
, pp. 3769-3773
-
-
Fang, N.1
Motto, D.G.2
Ross, S.E.3
Koretzky, G.A.4
-
45
-
-
0029832707
-
Differential regulation of activation-induced tyrosine phosphorylation and recruitment of SLP-76 to Vav by distinct isoforms of the CD45 protein-tyrosine phosphatase
-
of special interest. This study examines tyrosine phosphorylation and physical association of SLP-76 and p95Vav in Jurkat clones expressing distinct isoforms of CD45 protein tyrosine phosphatase. After TCR stimulation, Jurkat cells expressing the highest molecular weight isoform of CD45 show enhanced SLP-76 tyrosine phosphorylation and SLP-76-Vav association compared to cells expressing the lowest molecular weight CD45 isoform. Results suggest that CD45 isoform expression correlates with TCR-mediated association between SLP-76 and Vav.
-
Onodera H, Motto DG, Koretzky GA, Rothstein DM. Differential regulation of activation-induced tyrosine phosphorylation and recruitment of SLP-76 to Vav by distinct isoforms of the CD45 protein-tyrosine phosphatase. of special interest J Biol Chem. 271:1996;22225-22230 This study examines tyrosine phosphorylation and physical association of SLP-76 and p95Vav in Jurkat clones expressing distinct isoforms of CD45 protein tyrosine phosphatase. After TCR stimulation, Jurkat cells expressing the highest molecular weight isoform of CD45 show enhanced SLP-76 tyrosine phosphorylation and SLP-76-Vav association compared to cells expressing the lowest molecular weight CD45 isoform. Results suggest that CD45 isoform expression correlates with TCR-mediated association between SLP-76 and Vav.
-
(1996)
J Biol Chem
, vol.271
, pp. 22225-22230
-
-
Onodera, H.1
Motto, D.G.2
Koretzky, G.A.3
Rothstein, D.M.4
-
46
-
-
0029658306
-
P95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells
-
of special interest. This paper shows that stimulation of a T cell hybridoma with antigen-presenting cells induces association of p95Vav with phosphorylated SLP-76. Further, the SLP-76-Vav association is dependent on Vav SH2. The work suggests that a physiological stimulus induces endogenous SLP-76/Vav association.
-
Tuosto L, Michel F, Acuto O. p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells. of special interest J Exp Med. 184:1996;1161-1166 This paper shows that stimulation of a T cell hybridoma with antigen-presenting cells induces association of p95Vav with phosphorylated SLP-76. Further, the SLP-76-Vav association is dependent on Vav SH2. The work suggests that a physiological stimulus induces endogenous SLP-76/Vav association.
-
(1996)
J Exp Med
, vol.184
, pp. 1161-1166
-
-
Tuosto, L.1
Michel, F.2
Acuto, O.3
-
47
-
-
0001584956
-
Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation
-
of special interest. This work demonstrates that when tyrosine phosphorylated, the phosphoprotein SLP-76 binds to the Vav Src homology-2 (SH2) upon TCR stimulation (see also Onodera et al. [45] and Tuosto et al. [46]) in Jurkat T cells. Cooverexpression of SLP-76 and Vav synergistically augments TCR-induced IL-2 promoter activity.
-
Wu J, Motto DG, Koretzky GA, Weiss A. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. of special interest Immunity. 4:1996;593-602 This work demonstrates that when tyrosine phosphorylated, the phosphoprotein SLP-76 binds to the Vav Src homology-2 (SH2) upon TCR stimulation (see also Onodera et al. [45] and Tuosto et al. [46]) in Jurkat T cells. Cooverexpression of SLP-76 and Vav synergistically augments TCR-induced IL-2 promoter activity.
-
(1996)
Immunity
, vol.4
, pp. 593-602
-
-
Wu, J.1
Motto, D.G.2
Koretzky, G.A.3
Weiss, A.4
-
48
-
-
0030906543
-
Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCR zeta/CD3 induction of interleukin-2
-
Raab M, da Silva AJ, Findell PR, Rudd CE. Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCR zeta/CD3 induction of interleukin-2. Immunity. 6:1997;155-164.
-
(1997)
Immunity
, vol.6
, pp. 155-164
-
-
Raab, M.1
Da Silva, A.J.2
Findell, P.R.3
Rudd, C.E.4
-
49
-
-
0030959305
-
Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases
-
of outstanding interest. This study and that of da Silva et al., 1997 [50] describe the purification and cloning of SLAP-130/Fyb. Musci et al. utilize the phosphoprotein SLP-76 Src homology 2 (SH2) domain to isolate human SLAP-130/Fyb; da Silva et al. took purified SLAP-130/Fyb through its association with the SH2 domain of Fyn. In contrast to Musci et al., who find that SLAP-130/Fyb acts as an inhibitor of TCR-induced nuclear factor of activated T cells (NFAT) activity, da Silva et al. find that, when overexpressed in a T-cell hybridoma line, SLAP-130/Fyb causes a modest (three to fourfold) increase in TCR-stimulated IL-2 production.
-
Musci M, Hendricks-Taylor L, Motto D, Paskind M, Kamens J, Turck C, Koretzky G. Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases. of outstanding interest J Biol Chem. 272:1997;11674-11677 This study and that of da Silva et al., 1997 [50] describe the purification and cloning of SLAP-130/Fyb. Musci et al. utilize the phosphoprotein SLP-76 Src homology 2 (SH2) domain to isolate human SLAP-130/Fyb; da Silva et al. took purified SLAP-130/Fyb through its association with the SH2 domain of Fyn. In contrast to Musci et al., who find that SLAP-130/Fyb acts as an inhibitor of TCR-induced nuclear factor of activated T cells (NFAT) activity, da Silva et al. find that, when overexpressed in a T-cell hybridoma line, SLAP-130/Fyb causes a modest (three to fourfold) increase in TCR-stimulated IL-2 production.
-
(1997)
J Biol Chem
, vol.272
, pp. 11674-11677
-
-
Musci, M.1
Hendricks-Taylor, L.2
Motto, D.3
Paskind, M.4
Kamens, J.5
Turck, C.6
Koretzky, G.7
-
50
-
-
0030737886
-
Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production
-
of outstanding interest. This study and Musci et al., 1997 [49] describe the purification and cloning of SLAP-130/Fyb. Musci et al. utilize the phosphoprotein SLP-76 Src homomlogy 2 (SH2) domain to isolate human SLAP-130/Fyb; da Silva et al. took purified SLAP-130/Fyb through its association with the SH2 domain of Fyn. In contrast to Musci et al., who find that SLAP-130/Fyb acts as an inhibitor of TCR-induced nuclear factor of activated T cells (NFAT) activity, da Silva et al. find that when overexpressed in a T-cell hybridoma line, SLAP-130/Fyb causes a modest (three-to-fourfold) increase in TCR-stimulated IL-2 production.
-
Da Silva A, Li Z, De Vera C, Canto E, Findell P, Rudd C. Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production. of outstanding interest Proc Natl Acad Sci USA. 94:1997;7493-7498 This study and Musci et al., 1997 [49] describe the purification and cloning of SLAP-130/Fyb. Musci et al. utilize the phosphoprotein SLP-76 Src homomlogy 2 (SH2) domain to isolate human SLAP-130/Fyb; da Silva et al. took purified SLAP-130/Fyb through its association with the SH2 domain of Fyn. In contrast to Musci et al., who find that SLAP-130/Fyb acts as an inhibitor of TCR-induced nuclear factor of activated T cells (NFAT) activity, da Silva et al. find that when overexpressed in a T-cell hybridoma line, SLAP-130/Fyb causes a modest (three-to-fourfold) increase in TCR-stimulated IL-2 production.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 7493-7498
-
-
Da Silva, A.1
Li, Z.2
De Vera, C.3
Canto, E.4
Findell, P.5
Rudd, C.6
-
51
-
-
0031092695
-
Biochemical analysis of p120/130: A protein-tyrosine kinase substrate restricted to T and myeloid cells
-
Da Silva AJ, Rosenfield JM, Mueller I, Bouton A, Hirai H, Rudd CE. Biochemical analysis of p120/130: a protein-tyrosine kinase substrate restricted to T and myeloid cells. J Immunol. 158:1997;2007-2016.
-
(1997)
J Immunol
, vol.158
, pp. 2007-2016
-
-
Da Silva, A.J.1
Rosenfield, J.M.2
Mueller, I.3
Bouton, A.4
Hirai, H.5
Rudd, C.E.6
-
52
-
-
0030910820
-
Molecular cloning of SKAP55, a novel protein that associates with the protein tyrosine kinase p59fyn in human T-lymphocytes
-
of outstanding interest. A description of SKAP-55 purification and cloning via its association with the Src homology-2 (SH2) domain of Fyn. GST fusion protein analysis suggests that SKAP-55 binds selectively through phosphotyrosine to SH2 domains of Src family, but not Syk family protein tyrosine kinases. SKAP may mediate Fyn signaling.
-
Marie-Cardine A, Bruyns E, Eckerskorn C, Kirchgessner H, Meuer SC, Schraven B. Molecular cloning of SKAP55, a novel protein that associates with the protein tyrosine kinase p59fyn in human T-lymphocytes. of outstanding interest J Biol Chem. 272:1997;16077-16080 A description of SKAP-55 purification and cloning via its association with the Src homology-2 (SH2) domain of Fyn. GST fusion protein analysis suggests that SKAP-55 binds selectively through phosphotyrosine to SH2 domains of Src family, but not Syk family protein tyrosine kinases. SKAP may mediate Fyn signaling.
-
(1997)
J Biol Chem
, vol.272
, pp. 16077-16080
-
-
Marie-Cardine, A.1
Bruyns, E.2
Eckerskorn, C.3
Kirchgessner, H.4
Meuer, S.C.5
Schraven, B.6
-
53
-
-
0028180585
-
GRB2 and phospholipase C-gamma 1 associate with a 36- To 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation
-
Sieh M, Batzer A, Schlessinger J, Weiss A. GRB2 and phospholipase C-gamma 1 associate with a 36- to 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation. Mol Cell Biol. 14:1994;4435-4442.
-
(1994)
Mol Cell Biol
, vol.14
, pp. 4435-4442
-
-
Sieh, M.1
Batzer, A.2
Schlessinger, J.3
Weiss, A.4
-
54
-
-
0029999327
-
Tyrosine phosphorylation of Grb2-associated proteins correlates with phospholipase C-gamma-1 in T cells
-
Motto DG, Musci MA, Ross SE, Koretzky GA. Tyrosine phosphorylation of Grb2-associated proteins correlates with phospholipase C-gamma-1 in T cells. Mol Cell Biol. 16:1996;2823-2829.
-
(1996)
Mol Cell Biol
, vol.16
, pp. 2823-2829
-
-
Motto, D.G.1
Musci, M.A.2
Ross, S.E.3
Koretzky, G.A.4
-
55
-
-
0030886815
-
Impaired plasma membrane targeting of Grb2-murine son of sevenless (mSOS) complex and differential activation of the Fyn-T cell receptor (TCR)-zeta-Cbl pathway mediate T cell hyporesponsiveness in autoimmune nonobese diabetic mice
-
of outstanding interest. This paper examines T-cell hyporesponsiveness in non-obese diabetic mice. Decreased Ras pathway activity correlates with an enhanced Fyn/TCR-ζ/Cbl complex, decreased ZAP-70 and Grb2/Sos membrane targeting, and depressed phosphorylation of pp36. These data support the idea that pp36 (LAT) tyrosine phosphorylation is important for transducing activating TCR signals.
-
Salojin K, Zhang J, Cameron M, Gill B, Arreaza G, Ochi A, Delovitch TL. Impaired plasma membrane targeting of Grb2-murine son of sevenless (mSOS) complex and differential activation of the Fyn-T cell receptor (TCR)-zeta-Cbl pathway mediate T cell hyporesponsiveness in autoimmune nonobese diabetic mice. of outstanding interest J Exp Med. 186:1997;887-897 This paper examines T-cell hyporesponsiveness in non-obese diabetic mice. Decreased Ras pathway activity correlates with an enhanced Fyn/TCR-ζ/Cbl complex, decreased ZAP-70 and Grb2/Sos membrane targeting, and depressed phosphorylation of pp36. These data support the idea that pp36 (LAT) tyrosine phosphorylation is important for transducing activating TCR signals.
-
(1997)
J Exp Med
, vol.186
, pp. 887-897
-
-
Salojin, K.1
Zhang, J.2
Cameron, M.3
Gill, B.4
Arreaza, G.5
Ochi, A.6
Delovitch, T.L.7
-
56
-
-
0032498231
-
LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
-
of outstanding interest. of outstanding interest. A description of the purification, cloning and initial characterization of LAT. LAT is tyrosine phosphorylated upon TCR stimulation and binds to Grb2, SLP-76, phospholipase Cγ1 and phosphatidylinositol 3-kinase. Overexpressed tyrosine point mutants of LAT act as dominant interfering molecules for TCR stimulation of the nuclear factor of activated T cells (NFAT).
-
of outstanding interest Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE. LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. of outstanding interest Cell. 92:1997;83-92 A description of the purification, cloning and initial characterization of LAT. LAT is tyrosine phosphorylated upon TCR stimulation and binds to Grb2, SLP-76, phospholipase Cγ1 and phosphatidylinositol 3-kinase. Overexpressed tyrosine point mutants of LAT act as dominant interfering molecules for TCR stimulation of the nuclear factor of activated T cells (NFAT).
-
(1997)
Cell
, vol.92
, pp. 83-92
-
-
Zhang, W.1
Sloan-Lancaster, J.2
Kitchen, J.3
Trible, R.P.4
Samelson, L.E.5
-
57
-
-
0030812812
-
Maintenance of human T cell energy: Blocking of IL-2 gene transcription by activated Rap1
-
of outstanding interest. This study describes the association of T-cell anergy with altered membrane-proximal signaling complexes. Experiments show hyperphosphorylation of Cbl and recruitment of CrkL and C3G to Cbl in anergic cells. Enhanced GTP-bound Rap1 and recruitment of Raf to Rap1 are also specific for anergic cells, suggesting a mechanism for Ras pathway inhibition in induction of anergy.
-
Boussiotis VA, Freeman GJ, Berezovskaya A, Barber DL, Nadler LM. Maintenance of human T cell energy: blocking of IL-2 gene transcription by activated Rap1. of outstanding interest Science. 278:1997;124-128 This study describes the association of T-cell anergy with altered membrane-proximal signaling complexes. Experiments show hyperphosphorylation of Cbl and recruitment of CrkL and C3G to Cbl in anergic cells. Enhanced GTP-bound Rap1 and recruitment of Raf to Rap1 are also specific for anergic cells, suggesting a mechanism for Ras pathway inhibition in induction of anergy.
-
(1997)
Science
, vol.278
, pp. 124-128
-
-
Boussiotis, V.A.1
Freeman, G.J.2
Berezovskaya, A.3
Barber, D.L.4
Nadler, L.M.5
-
58
-
-
10144243337
-
A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells
-
Lupher ML Jr, Reedquist KA, Miyake S, Langdon WY, Band H. A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells. J Biol Chem. 271:1996;24063-24068.
-
(1996)
J Biol Chem
, vol.271
, pp. 24063-24068
-
-
Lupher M.L., Jr.1
Reedquist, K.A.2
Miyake, S.3
Langdon, W.Y.4
Band, H.5
-
59
-
-
0025819499
-
The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif
-
Blake TJ, Shapiro M, Morse HCD, Langdon WY. The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif. Oncogene. 6:1991;653-657.
-
(1991)
Oncogene
, vol.6
, pp. 653-657
-
-
Blake, T.J.1
Shapiro, M.2
Morse, H.C.D.3
Langdon, W.Y.4
-
60
-
-
0031178960
-
Proto-oncoprotein Vav interacts with c-Cbl in activated thymocytes and peripheral T cells
-
Marengere LE, Mirtsos C, Kozieradzki I, Veillette A, Mak TW, Penninger JM. Proto-oncoprotein Vav interacts with c-Cbl in activated thymocytes and peripheral T cells. J Immunol. 159:1997;70-76.
-
(1997)
J Immunol
, vol.159
, pp. 70-76
-
-
Marengere, L.E.1
Mirtsos, C.2
Kozieradzki, I.3
Veillette, A.4
Mak, T.W.5
Penninger, J.M.6
-
61
-
-
0029994305
-
Tyrosine-phosphorylated Cbl binds to Crk after T cell activation
-
Sawasdikosol S, Chang JH, Pratt JC, Wolf G, Shoelson SE, Burakoff SJ. Tyrosine-phosphorylated Cbl binds to Crk after T cell activation. J Immunol. 157:1996;110-116.
-
(1996)
J Immunol
, vol.157
, pp. 110-116
-
-
Sawasdikosol, S.1
Chang, J.H.2
Pratt, J.C.3
Wolf, G.4
Shoelson, S.E.5
Burakoff, S.J.6
-
62
-
-
0029034440
-
Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells
-
Meisner H, Conway BR, Hartley D, Czech MP. Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells. Mol Cell Biol. 15:1995;3571-3578.
-
(1995)
Mol Cell Biol
, vol.15
, pp. 3571-3578
-
-
Meisner, H.1
Conway, B.R.2
Hartley, D.3
Czech, M.P.4
-
63
-
-
0029998597
-
Specific association of tyrosine-phosphorylated c-Cbl with Fyn tyrosine kinase in T cells
-
Tsygankov AY, Mahajan S, Fincke JE, Bolen JB. Specific association of tyrosine-phosphorylated c-Cbl with Fyn tyrosine kinase in T cells. J Biol Chem. 271:1996;27130-27137.
-
(1996)
J Biol Chem
, vol.271
, pp. 27130-27137
-
-
Tsygankov, A.Y.1
Mahajan, S.2
Fincke, J.E.3
Bolen, J.B.4
-
64
-
-
0028027169
-
The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkst cells activated via the T cell antigen receptor
-
Donovan JA, Wange RL, Langdon WY, Samelson LE. The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkst cells activated via the T cell antigen receptor. J Biol Chem. 269:1994;22921-22924.
-
(1994)
J Biol Chem
, vol.269
, pp. 22921-22924
-
-
Donovan, J.A.1
Wange, R.L.2
Langdon, W.Y.3
Samelson, L.E.4
-
65
-
-
0029671073
-
P120cbl is a majo substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase
-
of special interest. This provides a demonstration of prominent B-cell receptor (BCR)-induced Cbl association with the protein tyrosine kinase Syk, and Cbl binding to Grb2, Shc, PI-3k, and Fyn. The data suggest that Cbl may affect signal transduction through the BCR.
-
Panchamoorthy G, Fukazawa T, Miyake S, Soltoff S, Reedquist K, Druker B, Shoelson S, Cantley L, Band H. p120cbl is a majo substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase. of special interest J Biol Chem. 271:1996;3187-3194 This provides a demonstration of prominent B-cell receptor (BCR)-induced Cbl association with the protein tyrosine kinase Syk, and Cbl binding to Grb2, Shc, PI-3k, and Fyn. The data suggest that Cbl may affect signal transduction through the BCR.
-
(1996)
J Biol Chem
, vol.271
, pp. 3187-3194
-
-
Panchamoorthy, G.1
Fukazawa, T.2
Miyake, S.3
Soltoff, S.4
Reedquist, K.5
Druker, B.6
Shoelson, S.7
Cantley, L.8
Band, H.9
-
66
-
-
0030712944
-
Cbl-mediated regulation of T cell receptor-induced AP1 activation
-
of special interest. This paper reports that overexpression of Cbl in Jurkat T cells can inhibit AP1 activity following TCR stimulation.
-
Rellahan B, Graham L, Stoica B, DeBell K, Bonvini E. Cbl-mediated regulation of T cell receptor-induced AP1 activation. of special interest J Biol Chem. 272:1997;30806-30811 This paper reports that overexpression of Cbl in Jurkat T cells can inhibit AP1 activity following TCR stimulation.
-
(1997)
J Biol Chem
, vol.272
, pp. 30806-30811
-
-
Rellahan, B.1
Graham, L.2
Stoica, B.3
Debell, K.4
Bonvini, E.5
-
67
-
-
0030889218
-
The product of the proto-oncogene c-cbl: A negative regulator of the Syk tyrosine kinase
-
of special interest. This demonstrates that overexpression of Cbl in the RBL mast cell line inhibits Syk kinase activity and serotonin release after stimulation through the IgE receptor FcεRI. The inhibition of Syk kinase activity is due to its binding to Cbl and subsequent dissociation from the immunoreceptor tyrosine-based activation motifs.
-
Ota Y, Samelson LE. The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase. of special interest Science. 276:1997;418-420 This demonstrates that overexpression of Cbl in the RBL mast cell line inhibits Syk kinase activity and serotonin release after stimulation through the IgE receptor FcεRI. The inhibition of Syk kinase activity is due to its binding to Cbl and subsequent dissociation from the immunoreceptor tyrosine-based activation motifs.
-
(1997)
Science
, vol.276
, pp. 418-420
-
-
Ota, Y.1
Samelson, L.E.2
-
68
-
-
14444276991
-
The cbl phosphotyrosine-binding domain selects a D(N/D)Xpy motif and binds to the tyr292 negative regulatory phosphorylation site of ZAP-70
-
of special interest. The authors show that the Cbl PTB domain recognition sequence is a motif that is present in ZAP-70; moreover, the recognition site for the Cbl PTB domain within ZAP-70 includes the tyrosine residue associated with negative regulation of ZAP-70 function. Point mutation of residues within the ZAP-70 recognition site removes that ability of Cbl to bind to ZAP-70 in vivo.
-
Lupher ML Jr, Songyang Z, Shoelson SE, Cantley LC, Band H. The cbl phosphotyrosine-binding domain selects a D(N/D)Xpy motif and binds to the tyr292 negative regulatory phosphorylation site of ZAP-70. of special interest J Biol Chem. 272:1997;33140-33144 The authors show that the Cbl PTB domain recognition sequence is a motif that is present in ZAP-70; moreover, the recognition site for the Cbl PTB domain within ZAP-70 includes the tyrosine residue associated with negative regulation of ZAP-70 function. Point mutation of residues within the ZAP-70 recognition site removes that ability of Cbl to bind to ZAP-70 in vivo.
-
(1997)
J Biol Chem
, vol.272
, pp. 33140-33144
-
-
Lupher M.L., Jr.1
Songyang, Z.2
Shoelson, S.E.3
Cantley, L.C.4
Band, H.5
-
69
-
-
0029876948
-
Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G
-
Reedquist KA, Fukazawa T, Panchamoorthy G, 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. 271:1996;8435-8442.
-
(1996)
J Biol Chem
, vol.271
, pp. 8435-8442
-
-
Reedquist, K.A.1
Fukazawa, T.2
Panchamoorthy, G.3
Langdon, W.Y.4
Shoelson, S.E.5
Druker, B.J.6
Band, H.7
-
70
-
-
0029768637
-
B cell antigen receptor signaling induces the formation of complexes containing the Crk adaptor proteins
-
Ingham RJ, Krebs DL, Barbazuk SM, Turck CW, Hirai H, Matsuda M, Gold MR. B cell antigen receptor signaling induces the formation of complexes containing the Crk adaptor proteins. J Biol Chem. 271:1996;32306-32314.
-
(1996)
J Biol Chem
, vol.271
, pp. 32306-32314
-
-
Ingham, R.J.1
Krebs, D.L.2
Barbazuk, S.M.3
Turck, C.W.4
Hirai, H.5
Matsuda, M.6
Gold, M.R.7
-
71
-
-
0027179910
-
Isolation and chromosomal localization of CRKL, a human crk-like gene
-
Ten Hoeve J, Morris C, Heisterkamp N, Groffen J. Isolation and chromosomal localization of CRKL, a human crk-like gene. Oncogene. 8:1993;2469-2474.
-
(1993)
Oncogene
, vol.8
, pp. 2469-2474
-
-
Ten Hoeve, J.1
Morris, C.2
Heisterkamp, N.3
Groffen, J.4
-
72
-
-
0030771490
-
Enhancement of guanine-nucleotide exchange activity of C3G for Rap1 by the expression of Crk, CrkL, and Grb2
-
of special interest. This provides an analysis of the Crk structural features required to enhance C3G guanine nucleotide exchange activity for Rap1. Both Src homology (SH)2 and SH3 domains of Crk are required, but membrane targeting of Crk can substitute for the SH2 domain, suggesting that recruitment of C3G to the cell membrane is a Crk function.
-
Ichiba T, Kuraishi Y, Sakai O, Nagata S, Groffen J, Kurata T, Hattori S, Matsuda M. Enhancement of guanine-nucleotide exchange activity of C3G for Rap1 by the expression of Crk, CrkL, and Grb2. of special interest J Biol Chem. 272:1997;22215-22220 This provides an analysis of the Crk structural features required to enhance C3G guanine nucleotide exchange activity for Rap1. Both Src homology (SH)2 and SH3 domains of Crk are required, but membrane targeting of Crk can substitute for the SH2 domain, suggesting that recruitment of C3G to the cell membrane is a Crk function.
-
(1997)
J Biol Chem
, vol.272
, pp. 22215-22220
-
-
Ichiba, T.1
Kuraishi, Y.2
Sakai, O.3
Nagata, S.4
Groffen, J.5
Kurata, T.6
Hattori, S.7
Matsuda, M.8
|