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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2003-1-16
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pubmed:abstractText |
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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12529439-10085298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12529439-10485851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12529439-10504335,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12529439-9950678
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1059-1524
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
230-40
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12529439-Actins,
pubmed-meshheading:12529439-Cell Division,
pubmed-meshheading:12529439-Centrosome,
pubmed-meshheading:12529439-Genes, Reporter,
pubmed-meshheading:12529439-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:12529439-HeLa Cells,
pubmed-meshheading:12529439-Humans,
pubmed-meshheading:12529439-Microtubules,
pubmed-meshheading:12529439-Protein Tyrosine Phosphatase, Non-Receptor Type 13,
pubmed-meshheading:12529439-Protein Tyrosine Phosphatases,
pubmed-meshheading:12529439-Recombinant Fusion Proteins,
pubmed-meshheading:12529439-Telophase,
pubmed-meshheading:12529439-Tubulin
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pubmed:year |
2003
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pubmed:articleTitle |
The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis.
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pubmed:affiliation |
Department of Molecular Neurobiochemistry, Ruhr-University Bochum, 44780 Bochum, Germany.
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