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© The Rockefeller University Press, 0021-9525/1997//845 $5.00
The Journal of Cell Biology, Volume 138, Number 4, , 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.

Abbreviations used in this paper: CTH, COOH-terminal homology; GST, glutathione-S-transferase; HA, hemagglutanin; HSCF, hematopoietic stem cell fraction; HSP, hematopoietic specific protein; PSTPIP, proline, serine, threonine phosphatase interacting protein; PTP, protein tyrosine phosphatases.

S. Utzig's salary is provided by Boehringer Ingelheim (Mannheim, Germany). The work was in part supported by grants from the Swiss Cancer League, and the Swiss National Science Foundation.

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