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PMID: 2494631 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Src homology 2 domain deletion mutants of p60v-src do not phosphorylate cellular proteins of 120-150 kDa.

Oncogene ·Vol. 4 ·No. 2 ·1989-02-00 ·Pages 231-6

Wendler PA, Boschelli F

Abstract

We have constructed seven deletions in the src homology 2 (SH2) domain of the Rous sarcoma virus src gene and have expressed them and wild-type v-src (wt v-src) in Rat 1 fibroblasts. Transfected cells containing mutant DNAs have reduced focus forming activity when compared to cells containing the wt v-src DNA. In most cases, established cell lines that express these mutants have altered growth properties in soft agar. The src proteins isolated from mutant cell lines have reduced tyrosine kinase activity. We also see differences in the phosphorylation of cellular proteins in vivo. Unlike the wt protein kinase, the SH2 domain mutant kinases do not phosphorylate a set of cellular proteins ranging in size from 120-150 kDa.

MeSH Terms
Animals Cell Transformation, Viral Chromosome Deletion Immunoblotting Oncogene Protein pp60(v-src) Oncogenes Phosphorylation Protein-Tyrosine Kinases/analysis Proteins/metabolism Rats Retroviridae Proteins/genetics,metabolism Transfection Tyrosine/metabolism
Chemicals
Proteins Retroviridae Proteins Tyrosine Protein-Tyrosine Kinases Oncogene Protein pp60(v-src)
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wendler P A
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Boschelli F
Article Info
Journal
Oncogene
Abbr.
Oncogene
ISSN
0950-9232
Published
1989-02-00
Pages
231-6
Language
English
Region
England
NLM ID
8711562
Subset
IM
Grants
NCI NIH HHS · 5RO1-CO-36928 · United States
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