Home LiteratureArticle Details
PMID: 3080999 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Phosphorylation of the cytoskeletal protein talin by protein kinase C.

Biochemical and biophysical research communications ·Vol. 134 ·No. 3 ·1986-02-13 ·Pages 1276-83

Litchfield DW, Ball EH

Abstract

Talin, a component of the focal contact of cultured cells, is an in vitro substrate for protein kinase C. Immunoprecipitation confirms that talin is the phosphorylated protein. Phosphorylation is dependent on both phosphatidylserine and calcium and reaches a level of incorporation of 0.8 mol phosphate/mol protein. Phosphoamino acid analysis demonstrates the presence of phosphoserine and phosphothreonine, but no phosphotyrosine. Two dimensional mapping of tryptic peptides, and V8 peptides reveals the existence of multiple phosphorylation sites. The identification of talin as a substrate for protein kinase C implicates talin as a potential regulator of focal contact organization and perhaps cell morphology.

MeSH Terms
Animals Autoradiography Chemical Precipitation Chickens Immunochemistry Muscle Proteins/metabolism Phosphorylation Protein Kinase C/metabolism Talin
Chemicals
Muscle Proteins Talin Protein Kinase C
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Litchfield D W
Ball E H
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1986-02-13
Pages
1276-83
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]