Back to Search Start Over

The Protein Tyrosine Phosphatase PTP-BL Associates with the Midbody and Is Involved in the Regulation of Cytokinesis

Authors :
Kai S. Erdmann
Thomas Dittmar
Lutz Herrmann
Source :
Molecular Biology of the Cell. 14:230-240
Publication Year :
2003
Publisher :
American Society for Cell Biology (ASCB), 2003.

Abstract

PTP-BL is a highly modular protein tyrosine phosphatase of unknown function. It consists of an N-terminal FERM domain, five PDZ domains, and a C-terminally located tyrosine phosphatase domain. Here we show that PTP-BL is involved in the regulation of cytokinesis. We demonstrate localization of endogenous PTP-BL at the centrosomes during inter- and metaphase and at the spindle midzone during anaphase. Finally PTP-BL is concentrated at the midbody in cytokinesis. We show that PTP-BL is targeted to the midbody and centrosome by a specific splicing variant of the N-terminus characterized by an insertion of 182 amino acids. Moreover, we demonstrate that the FERM domain of PTP-BL is associated with the contractile ring and can be cosedimented with filamentous actin, whereas the N-terminus can be cosedimented with microtubules. We demonstrate that elevating the expression level of wild-type PTP-BL or expression of PTP-BL with an inactive tyrosine phosphatase domain leads to defects in cytokinesis and to the generation of multinucleate cells. We suggest that PTP-BL plays a role in the regulation of cytokinesis.

Details

ISSN :
19394586 and 10591524
Volume :
14
Database :
OpenAIRE
Journal :
Molecular Biology of the Cell
Accession number :
edsair.doi.dedup.....485eaec7a9995d37b6a43ab2678de7be