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A more recent version of this article appeared on January 1, 2003
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Submitted on April 9, 2002
Revised on September 3, 2002
Accepted on September 13, 2002
1 Department of Molecular Neurobiochemistry, Ruhr-University Bochum, 44780 Bochum, Germany
2 Institute of Immunology, University Witten/Herdecke, 58448 Witten, Germany
* Corresponding author. E-mail address: kai.s.erdmann{at}ruhr-uni-bochum.de.
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 co-sedimented with filamentous actin, whereas the N-terminus can be co-sedimented with microtubules. We demonstrate that elevating the expression level of wildtype 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.
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