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PMID: 1639064 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity.

The EMBO journal ·Vol. 11 ·No. 8 ·1992-08-00 ·Pages 2919-24

Bergman M, Mustelin T, Oetken C, Partanen J, Flint NA, Amrein KE, Autero M, Burn P, Alitalo K

Abstract

Protein tyrosine kinases participate in the transduction and modulation of signals that regulate proliferation and differentiation of cells. Excessive or deregulated protein tyrosine kinase activity can cause malignant transformation. The catalytic activity of the T cell protein tyrosine kinase p56lck is normally suppressed by phosphorylation of a carboxyl-terminal tyrosine, Tyr-505, by another cellular protein tyrosine kinase. Here we characterize a human cytosolic 50 kDa protein tyrosine kinase, p50csk, which specifically phosphorylates Tyr-505 of p56lck and a synthetic peptide containing this site. Phosphorylation of Tyr-505 suppressed the catalytic activity of p56lck. We suggest that p50csk negatively regulates p56lck, and perhaps other cellular src family kinases.

MeSH Terms
Amino Acid Sequence CSK Tyrosine-Protein Kinase Homeostasis Humans Kinetics Lymphocyte Specific Protein Tyrosine Kinase p56(lck) Molecular Sequence Data Peptide Fragments/isolation & purification Peptide Mapping Phosphopeptides/isolation & purification Phosphotransferases Protein-Tyrosine Kinases/genetics,metabolism Proto-Oncogene Proteins/metabolism Recombinant Proteins/metabolism Substrate Specificity T-Lymphocytes/enzymology Transfection Trypsin Tyrosine src-Family Kinases
Chemicals
Peptide Fragments Phosphopeptides Proto-Oncogene Proteins Recombinant Proteins Tyrosine Phosphotransferases Protein-Tyrosine Kinases CSK Tyrosine-Protein Kinase Lymphocyte Specific Protein Tyrosine Kinase p56(lck) src-Family Kinases CSK protein, human Trypsin
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Bergman M
Department of Pathology, University of Helsinki, Finland.
Mustelin T
Oetken C
Partanen J
Flint N A
Amrein K E
Autero M
Burn P
Alitalo K
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1992-08-00
Pages
2919-24
Language
English
Region
England
NLM ID
8208664
PMCID
PMC556773
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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