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, 88 (16), 7242-6

Molecular Characterization of a Protein-Tyrosine-Phosphatase Enriched in Striatum

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Molecular Characterization of a Protein-Tyrosine-Phosphatase Enriched in Striatum

P J Lombroso et al. Proc Natl Acad Sci U S A.

Abstract

A cDNA clone encoding a neural-specific putative protein-tyrosine-phosphatase (protein-tyrosine-phosphate phosphohydrolase, EC 3.1.3.48) has been isolated from a rat striatal cDNA library. The deduced amino acid sequence predicts a protein of approximately 369 amino acids with a strong homology to other members of the family of protein-tyrosine-phosphatases. In vitro translation produces a protein with an apparent molecular mass of 46 kDa. A potential attachment mechanism to the cytoplasmic membrane is suggested by a myristoylation amino acid-consensus sequence at the N terminus of the protein. RNA analyses of various regions of rat brain reveal a 3-kilobase (kb) and a 4.4-kb mRNA. The 3-kb mRNA is highly enriched within the striatum relative to other brain areas and has been termed a "striatum enriched phosphatase" (STEP). In contrast, the 4.4-kb message is most abundant in the cerebral cortex and rare in the striatum. These two messages appear to be alternatively processed RNA transcripts of a single gene.

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References

    1. New Biol. 1990 Dec;2(12):1049-62 - PubMed
    1. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
    1. Annu Rev Biochem. 1985;54:897-930 - PubMed
    1. Methods Enzymol. 1987;152:219-27 - PubMed
    1. Proc Natl Acad Sci U S A. 1989 Nov;86(22):8698-702 - PubMed

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