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Control of cell motility by PTP-PEST

PTP-PEST is a cytoplasmic tyrosine phosphatase implicated in control of cell motility. Intriguingly, overexpression of PTP-PEST and deletion of the PTP-PEST gene both inhibit motility. The role of the phosphatase has therefore remained unclear, as has its mode of action — PTP-PEST contains binding sites for numerous proteins and therefore could function as an enzyme and/or a scaffold. Sarita Sastry and co-workers have examined the role of PTP-PEST in migrating CHOK1 and Rat1 cells (see p. 4305). They show that PTP-PEST transiently localizes to matrix-contact sites at the leading edge of migrating cells and that its activity increases following integrin-mediated attachment. They also show that PTP-PEST inhibits growth-factor-dependent cell migration, using a phosphatase-dead PTP-PEST mutant to demonstrate that this requires PTP-PEST phosphatase activity. Finally, the authors show that PTP-PEST suppresses integrin- and growth-factor-induced activation of Rac1 — a small GTPase required for cell migration — and that coexpression of activated Rac1 can alleviate the inhibitory effects of the phosphatase. Sastry and co-workers conclude that PTP-PEST, by inhibiting activation of Rac1, modulates signalling downstream of integrins and growth factor receptors to control lamellipodial protrusion.

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PTP-PEST controls motility through regulation of Rac1

Sarita K. Sastry, Patrick D. Lyons, Michael D. Schaller, and Keith Burridge
JCS 2002 115: 4305-4316. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?