Document Detail


Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon.
MedLine Citation:
PMID:  8618876     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The protein-tyrosine phosphatase epsilon (PTP epsilon) is a transmembranal, receptor-type protein that possesses two phosphatase catalytic domains characteristic of transmembranal phosphatases. Here we demonstrate the existence of a nontransmembranal isoform of PTP epsilon, PTP epsilon-cytoplasmic. PTP epsilon-cytoplasmic and the transmembranal isoform of PTP epsilon have separate, nonoverlapping expression patterns. Further, the data clearly indicate that control of which of the two isoforms is to be expressed is initiated at the transcriptional level, suggesting that they have distinct physiological roles. PTP epsilon-cytoplasmic mRNA is the product of a delayed early response gene in NIH 3T3 fibroblasts, and its transcription is regulated through a pathway that requires protein kinase C. The human homologue of PTP epsilon-cytoplasmic has also been cloned and is strongly up-regulated in the early stages of phorbol 12-tetradecanoate 13-acetate-induced differentiation of HL-60 cells. Sequence analysis indicates and cellular fractionation experiments confirm that this isoform is a cytoplasmic molecule. PTP epsilon-cytoplasmic is therefore the initial example to our knowledge of a nontransmembranal protein-tyrosine phosphatase that contains two tandem of catalytic domains.
Authors:
A Elson; P Leder
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  92     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1995 Dec 
Date Detail:
Created Date:  1996-06-07     Completed Date:  1996-06-07     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  12235-9     Citation Subset:  IM    
Affiliation:
Department of Genetics, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/U36623;  U36758
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Cell Differentiation
Cytoplasm / enzymology
DNA Primers
Enzyme Induction
Female
Genes, erbB-2
Genes, ras
Globins / biosynthesis,  genetics
HL-60 Cells
Humans
Isoenzymes / analysis,  biosynthesis
Mammary Glands, Animal / enzymology*
Mammary Tumor Virus, Mouse / genetics
Mice
Mice, Transgenic
Molecular Sequence Data
Oligonucleotide Probes
Polymerase Chain Reaction
Protein Tyrosine Phosphatases / analysis,  biosynthesis*
Receptor, erbB-2 / biosynthesis,  genetics
Sequence Homology, Amino Acid
Tetradecanoylphorbol Acetate / pharmacology*
Transcription, Genetic
Grant Support
ID/Acronym/Agency:
P20CA58203-02/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Isoenzymes; 0/Oligonucleotide Probes; 16561-29-8/Tetradecanoylphorbol Acetate; 9004-22-2/Globins; EC 2.7.10.1/Receptor, erbB-2; EC 3.1.3.48/Protein Tyrosine Phosphatases
Comments/Corrections

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