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Vol. 14, Issue 1, 230-240, January 2003

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

Lutz Herrmann,^* Thomas Dittmar, and Kai S. Erdmann^*

 ^*Department of Molecular Neurobiochemistry, Ruhr-University Bochum, 44780 Bochum, Germany; and  Institute of Immunology, University Witten/Herdecke, 58448 Witten, Germany

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.

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Online version of this article contains video material for Figure 7. Online version is available at www.molbiolcell.org.

Corresponding author. E-mail address: kai.s.erdmann{at}ruhr-uni-bochum.de.

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Molecular Biology of the Cell
Vol. 14, 230-240, January 2003
Copyright © 2003 by The American Society for Cell Biology

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