Format

Send to

Choose Destination
See comment in PubMed Commons below
Philos Trans R Soc Lond B Biol Sci. 1998 Apr 29;353(1368):583-605.

The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease.

Author information

  • 1Molecular Biology and Virology Laboratory, Salk Institute, La Jolla, CA 92037, USA.

Abstract

The reversible phosphorylation of tyrosines in proteins plays a key role in regulating many different processes in eukaryotic organisms, such as growth control, cell cycle control, differentiation cell shape and movement, gene transcription, synaptic transmission, and insulin action. Phosphorylation of proteins is brought about by enzymes called protein-tyrosine kinases that add phosphate to specific tyrosines in target proteins; phosphate is removed from phosphorylated tyrosines by enzymes called protein-tyrosine phosphatases. Phosphorylated tyrosines are recognized by specialized binding domains on other proteins, and such interactions are used to initiate intracellular signaling pathways. Currently, more than 95 protein-tyrosine kinases and more than 55 protein-tyrosine phosphatase genes are known in Homo sapiens. Aberrant tyrosine phosphorylation is a hallmark of many types of cancer and other human diseases. Drugs are being developed that antagonize the responsible protein-tyrosine kinases and phosphatases in order to combat these diseases.

PMID:
9602534
PMCID:
PMC1692245
DOI:
10.1098/rstb.1998.0228
[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center