J. Cell Biol.
© The Rockefeller University Press
0021-9525/97/08/845/16 $2.00
Volume 138, Number 4, August 25, 1997 845-860

PSTPIP: A Tyrosine Phosphorylated Cleavage Furrow-associated Protein that Is a Substrate for a PEST Tyrosine Phosphatase

Susan Spencer,^* Donald Dowbenko,^* Jill Cheng,^* Wenlu Li, Jennifer Brush,^§ Suzan Utzig, Viesturs Simanis,^¶ and Laurence A. Lasky^*

^* Department of Molecular Oncology,  Department of Pharmaceutical Sciences, and ^§ Department of Molecular Biology, Genentech, Inc., South San Francisco, California 94080; and ^¶ Cell Cycle Control Laboratory, Institut Suisse Recherches Expérimentales sur le Cancer, CH-1066 Epalinges, Switzerland

We have investigated proteins which interact with the PEST-type protein tyrosine phosphatase, PTP hematopoietic stem cell fraction (HSCF), using the yeast two-hybrid system. This resulted in the identification of proline, serine, threonine phosphatase interacting protein (PSTPIP), a novel member of the actin- associated protein family that is homologous to Schizosaccharomyces pombe CDC15p, a phosphorylated protein involved with the assembly of the actin ring in the cytokinetic cleavage furrow. The binding of PTP HSCF to PSTPIP was induced by a novel interaction between the putative coiled-coil region of PSTPIP and the COOH-terminal, proline-rich region of the phosphatase. PSTPIP is tyrosine phosphorylated both endogenously and in v-Src transfected COS cells, and cotransfection of dominant-negative PTP HSCF results in hyperphosphorylation of PSTPIP. This dominant-negative effect is dependent upon the inclusion of the COOH-terminal, proline-rich PSTPIP-binding region of the phosphatase. Confocal microscopy analysis of endogenous PSTPIP revealed colocalization with the cortical actin cytoskeleton, lamellipodia, and actin-rich cytokinetic cleavage furrow. Overexpression of PSTPIP in 3T3 cells resulted in the formation of extended filopodia, consistent with a role for this protein in actin reorganization. Finally, overexpression of mammalian PSTPIP in exponentially growing S. pombe results in a dominant-negative inhibition of cytokinesis. PSTPIP is therefore a novel actin-associated protein, potentially involved with cytokinesis, whose tyrosine phosphorylation is regulated by PTP HSCF.

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