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PMID: 7536343 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

FAP-1: a protein tyrosine phosphatase that associates with Fas.

Science (New York, N.Y.) ·Vol. 268 ·No. 5209 ·1995-04-21 ·Pages 411-5

Sato T, Irie S, Kitada S, Reed JC

Abstract

Fas is a cell surface receptor that controls a poorly understood signal transduction pathway that leads to cell death by means of apoptosis. A protein tyrosine phosphatase, FAP-1, capable of interacting with the cytosolic domain of Fas, was identified. The carboxyl terminal 15 amino acids of Fas are necessary and sufficient for interaction with FAP-1. FAP-1 expression is highest in tissues and cell lines that are relatively resistant to Fas-mediated cytotoxicity. Gene transfer-mediated elevations in FAP-1 partially abolished Fas-induced apoptosis in a T cell line. These findings are consistent with an inhibitory effect of FAP-1 on Fas signal transduction.

MeSH Terms
Amino Acid Sequence Animals Antigens, Surface/genetics,metabolism Apoptosis Base Sequence Cell Line Cloning, Molecular DNA, Complementary/genetics Humans Mice Molecular Sequence Data Protein Tyrosine Phosphatases/genetics,metabolism Receptors, Cell Surface/genetics,metabolism Recombinant Fusion Proteins/metabolism Signal Transduction T-Lymphocytes/cytology fas Receptor
Chemicals
Antigens, Surface DNA, Complementary Receptors, Cell Surface Recombinant Fusion Proteins fas Receptor Protein Tyrosine Phosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sato T
La Jolla Cancer Research Foundation, Oncogene and Tumor Suppressor Gene Program, CA 92037, USA.
Irie S
Kitada S
Reed J C
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1995-04-21
Pages
411-5
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Databases
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