Cloning and expression of two structurally distinct receptor-linked protein-tyrosine phosphatases generated by RNA processing from a single gene

Ming Gui Pan, Caroline Rim, Kun Ping Lu, Tullio Florio, Philip Stork

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We describe here the first example of RNA processing generating two functional receptor-linked protein-tyrosine phosphatases (PTP) (protein-tyrosine-phosphate phosphohydrolase, EC that are structurally distinct within their catalytic domains. Two cDNAs, PTP-P1 and PTP-PS, were isolated from rat pheochromocytoma cells, which encode two receptor-linked protein-tyrosine-phosphatases and are produced by alternative splicing and differential use of polyadenylation sites. Both cDNAs share an identical extracellular domain and a single transmembrane domain, but differ within their cytoplasmic regions: PTP-P1 contains two tandem repeated PTPase catalytic domains, whereas PTP-PS contains only the aminoterminal domain. Bacterial expression of PTPase domains of both cDNAs demonstrates that PTP-P1 and PTP-PS contain tyrosine-phosphatase activity. PTP-P1 is encoded by three transcripts of approximately 8, 6, and 4 kilobases, whereas PTP-PS is encoded by a single 4.8-kilobase transcript. PTP-Pl (6 kilobases) and PTP-PS are mainly expressed within the brain and in neuronal and endocrine cells. These data suggest that PTP-P1 and PTP-PS may be involved in neuronal function.

Original languageEnglish (US)
Pages (from-to)19284-19291
Number of pages8
JournalJournal of Biological Chemistry
Issue number26
Publication statusPublished - Sep 15 1993


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