| Title: |
PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase. |
| Authors: |
Spencer, S.; Dowbenko, D.; Cheng, J.; Li, W.; Brush, J.; Utzig, S.; Simanis, V.; Lasky, L.A. |
| Publication Year: |
1997 |
| Collection: |
Université de Lausanne (UNIL): Serval - Serveur académique lausannois |
| Subject Terms: |
3T3 Cells; Actins/metabolism; Adaptor Proteins; Signal Transducing; Amino Acid Sequence; Animals; Carrier Proteins/metabolism; Cell Cycle; Cytoskeletal Proteins/metabolism; Drug Interactions; Hematopoietic Cell Growth Factors/metabolism; Mice; Molecular Sequence Data; Phosphorylation; Protein Binding; Protein Tyrosine Phosphatase; Non-Receptor Type 12; Protein Tyrosine Phosphatases/biosynthesis; Protein Tyrosine Phosphatases/metabolism; Rats; Schizosaccharomyces/enzymology; Schizosaccharomyces/growth &; development; Subcellular Fractions/metabolism; Substrate Specificity; Tyrosine/metabolism |
| Description: |
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. |
| Document Type: |
article in journal/newspaper |
| File Description: |
application/pdf |
| Language: |
English |
| ISSN: |
0021-9525 |
| Relation: |
Journal of Cell Biology; https://iris.unil.ch/handle/iris/195120; serval:BIB_839; A1997XU36000010; 9265651 |
| DOI: |
10.1083/jcb.138.4.845 |
| Availability: |
https://iris.unil.ch/handle/iris/195120; https://doi.org/10.1083/jcb.138.4.845 |
| Accession Number: |
edsbas.A1C7CA6 |
| Database: |
BASE |