pubmed-article:12529439 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12529439 | lifeskim:mentions | umls-concept:C1167332 | lld:lifeskim |
pubmed-article:12529439 | lifeskim:mentions | umls-concept:C0085536 | lld:lifeskim |
pubmed-article:12529439 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:12529439 | lifeskim:mentions | umls-concept:C1419096 | lld:lifeskim |
pubmed-article:12529439 | lifeskim:mentions | umls-concept:C1819383 | lld:lifeskim |
pubmed-article:12529439 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:12529439 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:12529439 | pubmed:dateCreated | 2003-1-16 | lld:pubmed |
pubmed-article:12529439 | 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. | lld:pubmed |
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pubmed-article:12529439 | pubmed:language | eng | lld:pubmed |
pubmed-article:12529439 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12529439 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12529439 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12529439 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12529439 | pubmed:month | Jan | lld:pubmed |
pubmed-article:12529439 | pubmed:issn | 1059-1524 | lld:pubmed |
pubmed-article:12529439 | pubmed:author | pubmed-author:ErdmannKai... | lld:pubmed |
pubmed-article:12529439 | pubmed:author | pubmed-author:DittmarThomas... | lld:pubmed |
pubmed-article:12529439 | pubmed:author | pubmed-author:HerrmannLutzL | lld:pubmed |
pubmed-article:12529439 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12529439 | pubmed:volume | 14 | lld:pubmed |
pubmed-article:12529439 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12529439 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12529439 | pubmed:pagination | 230-40 | lld:pubmed |
pubmed-article:12529439 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:12529439 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12529439 | pubmed:articleTitle | The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis. | lld:pubmed |
pubmed-article:12529439 | pubmed:affiliation | Department of Molecular Neurobiochemistry, Ruhr-University Bochum, 44780 Bochum, Germany. | lld:pubmed |