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PMID: 2460746 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Regulation by the autophosphorylation site in overexpressed pp60c-src.

Molecular and cellular biology ·Vol. 8 ·No. 10 ·1988-10-00 ·Pages 4541-6

Kmiecik TE, Johnson PJ, Shalloway D

Abstract

We show that overexpressed pp60c-src is phosphorylated at Tyr-416 and has increased specific kinase activity when isolated from cells incubated with vanadate, a tyrosine phosphatase inhibitor. This supports the hypothesis that transient Tyr-416 phosphorylation modulates the activity of overexpressed pp60c-src in vivo. Mutagenesis indicates that Tyr-416 modulates pp60v-src activity as well.

MeSH Terms
Animals Mice Mutation Peptide Mapping Phosphorylation Phosphoserine/metabolism Phosphothreonine/metabolism Phosphotyrosine Protein-Tyrosine Kinases/metabolism Proto-Oncogene Proteins/metabolism Proto-Oncogene Proteins pp60(c-src) Structure-Activity Relationship Tyrosine/analogs & derivatives,metabolism Vanadium/pharmacology
Chemicals
Proto-Oncogene Proteins Vanadium Phosphothreonine Phosphoserine Phosphotyrosine Tyrosine Protein-Tyrosine Kinases Proto-Oncogene Proteins pp60(c-src)
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kmiecik T E
Department of Molecular and Cell Biology, Pennsylvania State University, University Park, 16802.
Johnson P J
Shalloway D
References (24)
24 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.8.10.4541-4546.1988
Published
1988-10-00
Pages
4541-6
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC365532
Subset
IM
Grants
NCI NIH HHS · CA32317 · United States
External Links
PubMed source DOI: 10.1128/mcb.8.10.4541-4546.1988 PMC Full Text View journal details
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