Work

The Protein-Tyrosine Kinase Substrate p36 Is Also a Substrate for Protein Kinase C In Vitro and In Vivo

Year: 1986

Type: article

Abstract: p36, a major in vivo substrate of protein-tyrosine kinases, is shown to be phosphorylated at serine 25, a site very close to the major site of tyrosine phosphorylation by pp60v-src, tyrosine 23 (J. R. Glenney, Jr., and B. F. Tack, Proc. Natl. Acad. Sci. USA 82:7884-7888, 1985). We present evidence suggesting that protein kinase C mediates phosphorylation of serine 25.

Source: Molecular and Cellular Biology

DOI: 10.1128/mcb.6.7.2738-2744.1986

Authors: K L Gould, J R Woodgett, C M Isacke, T Hunter

Institutions: Salk Institute for Biological Studies, University of California San Diego

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: Damon Runyon Cancer Research Foundation, National Institutes of Health, National Cancer Institute

Awards: VIRAL TRANSFORMING PROTEINS, MACROMOLECULAR SYNTHESIS AND GROWTH CONTROL