-
3
-
-
0026590736
-
Multiple SH2-Mediated Interactions in v-src Transformed Cells
-
of special interest, Using recombinant v-Src SH2 domains expressed as fusion proteins, the authors show that tyrosine phosphorylated targets of v-Src can bind to its SH2 domain. This illustrates the complexity and specificity of SH2-PTyr interactions and highlights the usefulness of fusion proteins as probes of SH2 function.
-
(1992)
Mol Cell Biol
, vol.12
, pp. 1366-1374
-
-
Koch1
Moran2
Anderson3
Lin4
Mbanalu5
Pawson6
-
7
-
-
0026572318
-
Effects of SH2 and SH3 Deletions on the Functional Activities of Wild-Type and Transforming Variants of c-Src
-
of special interest, Demonstrates that deletion of portions of the SH2 or SH3 domains activates c-Src and causes transformation of host cells. Illustrates the role of SH2 and SH3 domains in repressing c-Src activity in vivo.
-
(1992)
Mol Cell Biol
, vol.12
, pp. 1835-1845
-
-
Seidel-Dugan1
Mayer2
Thomas3
Brugge4
-
9
-
-
0025719212
-
c-src
-
of outstanding interest, This demonstration that the carboxy-terminal phosphopeptide binds to activated but not to wild-type c-Src provides the first direct support for the proposed model of c-Src regulation. Also illustrates the usefulness of phosphotyrosine-containing peptides as probes of SH2 domain function.
-
(1991)
Proc Natl Acad Sci USA
, vol.88
, pp. 10696-10700
-
-
Roussel1
Brodeur2
Shalloway3
Laudano4
-
12
-
-
0026612830
-
c-src During Mitosis
-
of special interest, Mutation of the three mitosis-specific phosphorylation sites in chicken c-Src reduces but does not abolish its mitotic activation. The results show that activation of c-Src is partly dependent on, but also partly independent of, its phosphorylation by Cdc2. This suggests a potential redundancy in regulation of c-Src and indicates the potential of regulation at other points in the cell cycle by amino-terminal phosphorylation and/or PTP/PTK regulation.
-
(1991)
Proceedings of the National Academy of Sciences
, vol.89
, pp. 7237-7241
-
-
Shenoy1
Chackalaparampil2
Bagrodia3
Lin4
Shalloway5
-
13
-
-
0026719599
-
Regulation of the cdc25 Protein During the Cell Cycle in Xenopus Extracts
-
(1992)
Cell
, vol.70
, pp. 139-151
-
-
Kumagai1
Dunphy2
-
14
-
-
0026528032
-
Coupling of Mitosis to the Completion of S Phase in Xenopus Occurs via Modulation of the Tyrosine Kinase that Phosphorylates p34cdc2
-
(1992)
Cell
, vol.68
, pp. 787-798
-
-
Smythe1
Newport2
-
16
-
-
0025766195
-
BCR-ABL Sequences Essential for Transformation by the BCR-ABL Oncogene Bind to the ABL SH2 Regulatory Domain in a Non-Phosphotyrosine-Dependent Manner
-
(1991)
Cell
, vol.66
, pp. 161-172
-
-
Pendergast1
Muller2
Havlik3
Maru4
Witte5
-
18
-
-
0009651402
-
The product of the Proto-Oncogene c-src is Modified During the Cellular Response to Platelet-Derived Growth Factor
-
(1985)
Proc Natl Acad Sci USA
, vol.82
, pp. 7845-7849
-
-
Ralston1
Bishop2
-
21
-
-
0026668932
-
Association of Fyn with the Activated Platelet-Derived Growth Factor Receptor: Requirements for Binding and Phosphorylation
-
(1992)
Oncogene
, vol.7
, pp. 1893-1901
-
-
Twamley1
Kypta2
Hall3
Courtneidge4
-
24
-
-
0026793393
-
Activated Src Tyrosine Kinase Phosphorylates Tyr 457 of Bovine GTPase — Activating Protein (GAP) in Vitro and the Corresponding Residue of Rat GAP in Vivo
-
(1992)
J Biol Chem
, vol.267
, pp. 17194-17200
-
-
Park1
Lin2
Pawson3
Jove4
-
28
-
-
0026612411
-
fyn Mutant Mice Display Differential Signaling in Thymocytes and Peripheral T Cells
-
of special interest, Targeted disruption of the fyn gene demonstrates that its product is a critical component of the TCR signaling pathway in thymocytes, but that its loss may be compensated for in mature peripheral T cells.
-
(1992)
Cell
, vol.70
, pp. 741-750
-
-
Stein1
Lee2
Rich3
Soriano4
-
31
-
-
0026705903
-
Genetic Evidence for the Involvement of the lck Tyrosine Kinase in Signal Transduction Through the T Cell Antigen Receptor
-
of special interest, A previously characterized T-cell line defective in TCR signaling is shown to lack functional Lck, indicating its involvement in this process.
-
(1992)
Cell
, vol.70
, pp. 585-593
-
-
Straus1
Weiss2
-
32
-
-
0025297050
-
Tyrosine Phosphatase CD45 is Essential for Couping T-Cell Antigen to the Phosphatidyl Inositol Pathway
-
(1990)
Nature
, vol.346
, pp. 66-68
-
-
Koretsky1
Picus2
Thomas3
Weiss4
-
33
-
-
0026341507
-
Phosphorylation of c-src on Tyrosine by Another Protein Tyrosine Kinase
-
of special interest, Kinase-defective c-Src (Lys295Arg) is phosphorylated at its carboxy-terminal regulatory tyrosine residue in cells lacking endogenous c-Src. Provides a convincing demonstration that c-Src can be phosphorylated at its regulatory tyrosine by another tyrosine kinase.
-
(1991)
Science
, vol.254
, pp. 568-571
-
-
Thomas1
Soriano2
Brugge3
-
37
-
-
0026568155
-
Molecular Cloning and Expression of Chicken C-terminal Src Kinase: Lack of Stable Association with c-Src Protein
-
of special interest, The absence of cross-hybridization in Southern-blot analysis under low stringency conditions suggests that the gene encoding the carboxy-terminal Src kinase, Csk, is not a member of a gene family.
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 2190-2194
-
-
Sabe1
Knudsen2
Okada3
Nada4
Nakagawa5
Hanafusa6
-
38
-
-
0026355723
-
CSK: A Protein-Tyrosine Kinase Involved in Regulation of src Family Kinases
-
of special interest, As well as phosphorylating the carboxy-terminal regulatory tyrosine of c-Src in vitro, Csk phosphorylates the equivalent residues of the Lyn and Fyn kinases and down-regulates their activities. Together with [37], demonstrates the ubiquitous tissue distribution of Csk.
-
(1991)
J Biol Chem
, vol.266
, pp. 24249-24252
-
-
Okada1
Nada2
Yamanashi3
Yamamoto4
Nakagawa5
-
39
-
-
0026681275
-
lck at Tyr505 and Down Regulates its Catalytic Activity
-
of special interest, Demonstrates that Csk also phosphorylates the Src family kinase Lck at its regulatory tyrosine. Together with [37,38], illustrates the central importance of Csk in potentially regulating all Src-family tyrosine kinases.
-
(1992)
EMBO J
, vol.11
, pp. 2919-2924
-
-
Bergman1
Mustelin2
Oetken3
Partanen4
Flint5
Amrein6
Antero7
Burn8
Alitalo9
-
40
-
-
0026648707
-
Activation of c-Src in Cells Bearing v-Crk and its Suppression by Csk
-
of outstanding interest, The first evidence that Csk can down-regulate activated c-Src in vivo. Also shows that v-Crk-mediated transformation is at least in part the result of c-Src activation. Illustrates the potential of Csk as a tumor-suppressor gene product.
-
(1992)
Mol Cell Biol
, vol.12
, pp. 4706-4713
-
-
Sabe1
Okada2
Nakagawa3
Hanafusa4
-
42
-
-
0026705734
-
c-src by Overexpression of a Protein Tyrosine Phosphatase
-
of outstanding interest, An important study identifying the receptor-like PTPα as a potential activator of c-Src. This is the first demonstration of a cellular protein that can directly regulate c-Src both in vitro and in vivo, and the first report of a tyrosine phosphatase possessing oncogenic potential.
-
(1992)
Nature
, vol.359
, pp. 336-339
-
-
Zheng1
Wang2
Pallen3
-
43
-
-
0025816584
-
A Protein Tyrosine Phosphatase with Sequence Similarity to the SH2 Domain of the Protein Tyrosine Kinases
-
(1991)
Nature
, vol.352
, pp. 736-742
-
-
Shen1
Bastien2
Posner3
Chretien4
-
44
-
-
0026630991
-
Corkscrew Encodes a Putative Protein Tyrosine Phosphatase that Functions to Transduce the Terminal Signal from the Receptor Tyrosine Kinase torso
-
(1992)
Cell
, vol.70
, pp. 225-236
-
-
Perkins1
Larsen2
Perrimon3
-
46
-
-
0026786471
-
Regulation of Protein Serine-Threonine Phosphatase Type 2A by Tyrosine Phosphorylation
-
(1992)
Science
, vol.257
, pp. 1261-1264
-
-
Chen1
Martin2
Brautigan3
-
48
-
-
0026612521
-
FAK, a Structurally Distinctive Protein-Tyrosine Kinase Associated with Focal Adhesions
-
of special interest, Introduces a member of a new class of protein tyrosine kinases, FAK, which may be regulated by Src and by integrin-mediated signals.
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 5192-5196
-
-
Schaller1
Borgman2
Cobb3
Vines4
Reynolds5
Parsons6
-
49
-
-
0026759309
-
Regulation of Focal Adhesion-Associate Protein Tyrosine Kinase by Both Cellular Adhesion and Oncogenic Transformation
-
of special interest, Direct demonstration that FAK is tyrosine phosphorylated and activated both by fibronectin-integrin signaling and by Src-mediated transformation. Together with [48,50–52], suggests a potential role for FAK in Src signaling, and of Src in integrin signaling.
-
(1992)
Nature
, vol.358
, pp. 690-692
-
-
Guan1
Shalloway2
-
52
-
-
0026445719
-
FAK Accompanies Cell Adhesion to Extracellular Matrix: A Role in Cytoskeletal Assembly
-
(1992)
J Cell Biol
, vol.119
, pp. 893-903
-
-
Burridge1
Turner2
Romer3
-
53
-
-
0026611047
-
c-src with Edosomal Membranes in Mammalian Fibroblasts
-
of outstanding interest, A significant report that convincingly demonstrates the localization of c-Src in mammalian fibroblasts to endosomes, which, in turn, associate with microtubular structures. These results and those of [54] suggest potential roles of c-Src in endosome regulation and perhaps protein trafficking.
-
(1992)
J Cell Biol
, vol.118
, pp. 321-333
-
-
Kaplan1
Swedlow2
Varmus3
Morgan4
-
61
-
-
0027340192
-
c-src to Integrin-Dependent Cytoskeletal Complexes in Throm bin-Stimulated Platelets
-
in press
-
(1993)
Mol Cell Biol
-
-
Clark1
Brugge2
-
65
-
-
0025905180
-
Keeping Track of Neurotrophin Receptors
-
(1991)
Cell
, vol.65
, pp. 915-918
-
-
Bothwell1
-
67
-
-
0025931499
-
Signal Transduction by Nerve Growth Factor and Fibroblast Growth Factor in PC12 Cells Requires a Sequence of Src and Ras Actions
-
of special interest, Using neutralized antibodies, it is shown that c-Src appears to function downstream of the NGF receptor and upstream of Ras in NGF-induced differentiation of PC12 cells. The study also has broader implications for the role of c-Src in mediating growth factor responses in proliferating cells.
-
(1991)
J Cell Biol
, vol.115
, pp. 809-819
-
-
Kremer1
D'Arcangelo2
Thomas3
DeMarco4
Brugge5
Halegona6
-
68
-
-
0026609632
-
c-src Tyrosine Kinase Modulates P19 Embryonal Carcinoma Cell Fate by Inhibiting Neuronal but not Epithelial Differentiation
-
(1992)
J Cell Biol
, vol.116
, pp. 1019-1033
-
-
Schmidt1
Brugge2
Nelson3
-
69
-
-
0026698924
-
Crystal structure of the Phosphotyrosine Recognition Domain SH2 of v-src Complexed with Tyrosine-Phosphorylated Peptides
-
of outstanding interest, The resolution of the crystal structure of v-Src's SH2 domain, together with the SH2 domain solution structures in [70,71], provides the basis for the design of specific inhibitors or modulators of SH2 domain-phosphoprotein interactions. Such modulators will be invaluable probes of SH2 function in normal cell growth and oncogenic transformation. Both this paper and [70] are accompanied, in the same issue of Nature, by an illuminating discussion of their results and their significance.
-
(1992)
Nature
, vol.358
, pp. 646
-
-
Waksman1
Kominos2
Robertson3
Pant4
Baltimore5
Birge6
Cowburn7
Hanafusa8
Mayer9
Overduin10
-
72
-
-
0026484261
-
SH2 and SH3 Domains: From Structure to Function
-
(1992)
Cell
, vol.71
, pp. 359-362
-
-
Pawson1
Gish2
|