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PMID: 8355678 Published · ppublish English Journal Article

Structure, mapping, and expression of erp, a growth factor-inducible gene encoding a nontransmembrane protein tyrosine phosphatase, and effect of ERP on cell growth.

Molecular and cellular biology ·Vol. 13 ·No. 9 ·1993-09-00 ·Pages 5195-205

Noguchi T, Metz R, Chen L, Mattéi MG, Carrasco D, Bravo R

Abstract

We have characterized a growth factor-inducible gene, erp, and demonstrated that it encodes a 367-amino-acid nontransmembrane tyrosine phosphatase protein with significant similarity to the vaccinia virus H1 protein. Immunoprecipitation analyses show that the erp protein, ERP, is rapidly induced following serum stimulation of quiescent fibroblasts. ERP has been expressed as a fusion protein with glutathione S-transferase and shown to have tyrosine as well as serine protein phosphatase activity. The enzymatic activity of ERP depends on the presence of reducing agents such as dithiothreitol, and its tyrosine phosphatase activity is inhibited by sodium vanadate, a potent inhibitor of protein tyrosine phosphatases. The number of stable NIH 3T3 clones obtained after transfection with a vector expressing the complete ERP protein is reduced more than 90% compared with that after transfection with a vector expressing a mutated inactive ERP protein. The remaining ERP-expressing clones present a significant increase in the proportion of bi- and multinucleated cells and a decrease in proliferation rate. Studies on the genomic structure reveal that the erp transcription unit is 2.8 kbp long and split into four exons. The erp gene maps to the 17A2-17C region of the murine genome. Our results demonstrate that the protein product of the immediate-early gene erp has a negative effect on cell proliferation.

Related Genes
erp
MeSH Terms
3T3 Cells Amino Acid Sequence Animals Base Sequence Cell Division Cell Survival Chromosome Mapping Cloning, Molecular DNA/genetics Gene Expression Regulation, Enzymologic Growth Substances/pharmacology Lung/enzymology Mice Molecular Sequence Data Oligodeoxyribonucleotides/chemistry Protein Tyrosine Phosphatases/metabolism RNA, Messenger/genetics Substrate Specificity
Chemicals
Growth Substances Oligodeoxyribonucleotides RNA, Messenger DNA Protein Tyrosine Phosphatases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Noguchi T
Department of Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey 08543-4000.
Metz R
Chen L
Mattéi M G
Carrasco D
Bravo R
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.13.9.5195-5205.1993
Published
1993-09-00
Pages
5195-205
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC360208
Subset
IM
External Links
PubMed source DOI: 10.1128/mcb.13.9.5195-5205.1993 PMC Full Text View journal details
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