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PMID: 3097514 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Features of the pp60v-src carboxyl terminus that are required for transformation.

Molecular and cellular biology ·Vol. 6 ·No. 8 ·1986-08-00 ·Pages 2807-19

Yaciuk P, Shalloway D

Abstract

Analysis of the biological and biochemical activities of pp60recombinant-src proteins encoded by 12 carboxyl-terminal mutants showed that a wide family of alternate src carboxyl termini permit complete transforming and kinase activities. src proteins having carboxyl termini which are up to 10 amino acids longer than that of pp60c-src (17 amino acids longer than that of pp60v-src) still permit transformation. Transformation-positive mutations preserve leucine-516, a residue which is highly conserved in protein-tyrosine kinase sequences; removal causes in vivo protein instability. Successive deletion mutants show that this residue is at the boundary of a region required for kinase activity. pp60src which is truncated just outside this point still transforms cells and binds both pp50 and pp90 cellular proteins.

MeSH Terms
Amino Acid Sequence Animals Cell Transformation, Neoplastic Mice Mutation Oncogene Protein pp60(v-src) Phosphoproteins/metabolism Plasmids Protein-Tyrosine Kinases/metabolism Retroviridae Proteins/analysis,genetics Structure-Activity Relationship
Chemicals
Phosphoproteins Retroviridae Proteins Protein-Tyrosine Kinases Oncogene Protein pp60(v-src)
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Yaciuk P
Shalloway D
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.6.8.2807-2819.1986
Published
1986-08-00
Pages
2807-19
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC367848
Subset
IM
Grants
NCI NIH HHS · CA32317 · United States
External Links
PubMed source DOI: 10.1128/mcb.6.8.2807-2819.1986 PMC Full Text View journal details
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