Journal ArticleDOI
PDGF β-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with a signaling complex
David R. Kaplan,Deborah K. Morrison,Gail Wong,Frank McCormick,Lewis T. Williams,Lewis T. Williams +5 more
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TLDR
The association of GAP with ligand-activated PDGF receptors may directly link PDGF and ras signaling pathways and suggest that PDGF induced the formation of complexes of signaling molecules.About:
This article is published in Cell.The article was published on 1990-04-06. It has received 492 citations till now. The article focuses on the topics: Tyrosine phosphorylation & Platelet-derived growth factor receptor.read more
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Oncogenes and signal transduction
Lewis C. Cantley,Kurt R. Auger,Christopher L. Carpenter,Brian C. Duckworth,Andrea Graziani,Rosana Kapeller,Stephen P. Soltoff +6 more
TL;DR: The protein-tyrosine kinase oncogenes will be the primary focus of the review as discussed by the authors, however, biochemical connections between the protein tyrosine Kinases and oncoproteins of the Ras,Raf,Fos,Jun, and Rel families as well as the protein kinase C family are also discussed.
Journal ArticleDOI
Small GTP-Binding Proteins
TL;DR: In this review, functions of small G proteins and their modes of activation and action are described.
Journal ArticleDOI
The GTPase superfamily: a conserved switch for diverse cell functions
TL;DR: A molecular switch is a molecular switch whose "on" and "off" states are triggered by binding and hydrolysis of GTP as discussed by the authors. But the mechanism in myriad versions of the switch can be traced back to a single primordial protein.
Journal ArticleDOI
Molecular themes in oncogenesis
TL;DR: It seems likely that most malignancies arise from the collaborative effects of dominant and recessive lesions, andumeration of the number of tumor suppressor genes afflicted in any given tumor may be greater.
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The trk proto-oncogene product: a signal transducing receptor for nerve growth factor
TL;DR: Affinity cross-linking and equilibrium binding experiments with 125I-labeled NGF indicate that p140prototrk binds NGF specifically in cultured cells with a dissociation constant of 10(-9) molar.
References
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Journal ArticleDOI
Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors
Yosef Yarden,Jaime Escobedo,Wun-Jing Kuang,Teresa L. Yang-Feng,T. O. Daniel,P. M. Tremble,Ellson Y. Chen,M. E. Ando,Richard N. Harkins,Uta Francke,Victor A. Fried,Axel Ullrich,Lewis T. Williams +12 more
TL;DR: The primary structure of the receptor for platelet-derived growth factor (PDGF), determined by means of cloning a cDNA that encodes the murine pre-PDGF receptor, is closely related to that of the v-kit oncogene product and the receptors for macrophage colony stimulating factor (CSF-1).
Journal ArticleDOI
A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants
Meg Trahey,Frank McCormick +1 more
TL;DR: In Xenopus oocytes, this protein maintains normal p21 in a biologically inactive, GDP-bound state through its effect on GTPase activity, and it appears that the major effect of position 12 mutations is to prevent this protein from stimulating p21 GTP enzyme activity, thereby allowing these mutants to remain in the active GTP- bound state.
Journal ArticleDOI
PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells.
TL;DR: Both the temporal production of these novel phospholipids after PDGF stimulation and the observation of the enzymatic activities that produce them in alpha-P-tyr immunoprecipitates suggest that these phospholIPids are excellent candidates for mediators of the PDGF mitogenic response.
Journal ArticleDOI
Phospholipase C-γ is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro
TL;DR: It is proposed that tyrosine phosphorylation of PLC-γ by PDGF and EGF receptors leads to its activation, and a consequent increase in phosphatidylinositol turnover.
Journal ArticleDOI
Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells.
TL;DR: It is reported here that NIH 3T3 cells induced to divide by adding serum to the culture medium are unable to enter the S phase of the cell cycle after microinjection of anti-ras antibody, showing that the protein product of the ras proto-oncogene is required for initiation of the S-phase in NIH 3 T3 cells.
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Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases
Signal transduction by receptors with tyrosine kinase activity
Axel Ullrich,Joseph Schlessinger +1 more