Literature DB >> 2069873

Mechanism of activation of the vav protooncogene.

J Coppola1, S Bryant, T Koda, D Conway, M Barbacid.   

Abstract

vav is a human locus that appears to be specifically expressed in cells of hematopoietic origin regardless of their differentiation lineage. This gene was first identified as a result of its malignant activation during the course of gene transfer assays (Katzav, S., Martin-Zanca, D., and Barbacid, M. EMBO J., 8: 2283-2290, 1989). In this study, we report the isolation of complementary DNA clones containing the entire coding sequence of the mouse vav protooncogene. Antisera raised against a peptide corresponding to a predicted hydrophilic domain have allowed us to identify the product of the vav gene as a 95,000 Da protein. Analysis of the deduced amino acid sequence of p95vav revealed an amino-terminal leucine-rich region not present in the activated vav oncogene. This region consists of an amphipathic helix-loop-helix followed by a leucine zipper, a structure reminiscent of the carboxy-terminal region of myc proteins and the steroid binding domain of nuclear receptors. In vitro mutagenicity studies have indicated that removal of the amphipathic helix-loop-helix is sufficient to activate the transforming potential of human and mouse vav protooncogenes. vav proteins also possess a cysteine-rich domain whose sequence predicts the formation of two putative metal binding-like domains, Cys-X2-Cys-X13-Cys-X2-Cys and His-X2-Cys-X6-Cys-X2-His. Replacement of some of these cysteine and histidine residues completely abolished the transforming activity of vav genes. Further examination of the alignment of cysteine residues in this region revealed an alternative structure, Cys-X2-Cys-X13-Cys-X2-Cys-X7-Cys-X6-Cys, which is reminiscent of the phorbol ester binding domain of protein kinase C. A similar domain has been recently identified in a second enzyme, diacylglycerol kinase. These structural similarities, along with its expression pattern, suggest that the vav protooncogene codes for a new type of signal-transducing molecule that may play an important role in controlling hematopoiesis.

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Year:  1991        PMID: 2069873

Source DB:  PubMed          Journal:  Cell Growth Differ        ISSN: 1044-9523


  39 in total

Review 1.  Regulatory and signaling properties of the Vav family.

Authors:  X R Bustelo
Journal:  Mol Cell Biol       Date:  2000-03       Impact factor: 4.272

2.  Critical but distinct roles for the pleckstrin homology and cysteine-rich domains as positive modulators of Vav2 signaling and transformation.

Authors:  Michelle A Booden; Sharon L Campbell; Channing J Der
Journal:  Mol Cell Biol       Date:  2002-04       Impact factor: 4.272

3.  Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation.

Authors:  L Zeng; P Sachdev; L Yan; J L Chan; T Trenkle; M McClelland; J Welsh; L H Wang
Journal:  Mol Cell Biol       Date:  2000-12       Impact factor: 4.272

4.  Mechanistic analysis of the amplification and diversification events induced by Vav proteins in B-lymphocytes.

Authors:  María J Caloca; José L Zugaza; Xosé R Bustelo
Journal:  J Biol Chem       Date:  2008-10-29       Impact factor: 5.157

5.  Lck regulates Vav activation of members of the Rho family of GTPases.

Authors:  J Han; B Das; W Wei; L Van Aelst; R D Mosteller; R Khosravi-Far; J K Westwick; C J Der; D Broek
Journal:  Mol Cell Biol       Date:  1997-03       Impact factor: 4.272

6.  Constitutive Bcl-2 expression throughout the hematopoietic compartment affects multiple lineages and enhances progenitor cell survival.

Authors:  S Ogilvy; D Metcalf; C G Print; M L Bath; A W Harris; J M Adams
Journal:  Proc Natl Acad Sci U S A       Date:  1999-12-21       Impact factor: 11.205

7.  Binding of Vav to Grb2 through dimerization of Src homology 3 domains.

Authors:  Z S Ye; D Baltimore
Journal:  Proc Natl Acad Sci U S A       Date:  1994-12-20       Impact factor: 11.205

8.  Phosphorylation-dependent and constitutive activation of Rho proteins by wild-type and oncogenic Vav-2.

Authors:  K E Schuebel; N Movilla; J L Rosa; X R Bustelo
Journal:  EMBO J       Date:  1998-11-16       Impact factor: 11.598

9.  Molecular cloning of the mouse grb2 gene: differential interaction of the Grb2 adaptor protein with epidermal growth factor and nerve growth factor receptors.

Authors:  K L Suen; X R Bustelo; T Pawson; M Barbacid
Journal:  Mol Cell Biol       Date:  1993-09       Impact factor: 4.272

10.  Diacylglycerol-dependent binding recruits PKCtheta and RasGRP1 C1 domains to specific subcellular localizations in living T lymphocytes.

Authors:  Silvia Carrasco; Isabel Merida
Journal:  Mol Biol Cell       Date:  2004-04-02       Impact factor: 4.138

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