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Stimulation of receptor protein-tyrosine phosphatase alpha activity and phosphorylation by phorbol ester



Stimulation of receptor protein-tyrosine phosphatase alpha activity and phosphorylation by phorbol ester



Cell Growth and Differentiation 6(3): 303-307



Receptor Protein-Tyrosine Phosphatase alpha (RPTP-alpha) is a transmembrane protein with two cytoplasmic catalytic protein-tyrosine phosphatase (PTP) domains and a relatively short (123 amino acids) extracellular domain. Here we report that treatment of transfected cells that express RPTP-alpha with the phorbol ester 12-O-tetradecanoyl-phorbol-13-acetate, a direct activator of protein kinase C, induced a rapid, transient increase in RPTP-alpha activity due to a 2- to 3-fold increase in substrate affinity. A transient increase in RPTP-alpha serine phosphorylation was concomitant with the enhanced activity. Tryptic phosphopeptide mapping of RPTP-alpha demonstrated that phosphorylation of three tryptic peptides was enhanced in response to phorbol ester. In vitro dephosphorylation of RPTP-alpha from phorbol ester-treated cells reduced RPTP-alpha activity to prestimulation levels, indicating that enhanced serine phosphorylation directly accounted for the increase in activity. Our results demonstrate that serine phosphorylation may play a key role in the regulation of the activity of transmembrane PTPs.

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Accession: 009459012

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PMID: 7794797


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