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pubmed-article:12529439pubmed:abstractTextPTP-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.lld:pubmed
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pubmed-article:12529439pubmed:authorpubmed-author:ErdmannKai...lld:pubmed
pubmed-article:12529439pubmed:authorpubmed-author:DittmarThomas...lld:pubmed
pubmed-article:12529439pubmed:authorpubmed-author:HerrmannLutzLlld:pubmed
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pubmed-article:12529439pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:12529439pubmed:articleTitleThe protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis.lld:pubmed
pubmed-article:12529439pubmed:affiliationDepartment of Molecular Neurobiochemistry, Ruhr-University Bochum, 44780 Bochum, Germany.lld:pubmed
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