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The Protein Tyrosine Phosphatase PTP-BL Associates with the Midbody and Is Involved in the Regulation of Cytokinesis
- Source :
- Molecular Biology of the Cell. 14:230-240
- Publication Year :
- 2003
- Publisher :
- American Society for Cell Biology (ASCB), 2003.
-
Abstract
- 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.
- Subjects :
- animal structures
Recombinant Fusion Proteins
PDZ domain
Protein Tyrosine Phosphatase, Non-Receptor Type 13
Protein tyrosine phosphatase
Biology
Microtubules
environment and public health
Filamentous actin
Article
Genes, Reporter
Tubulin
Guanine Nucleotide Exchange Factors
Humans
Telophase
Molecular Biology
Actin
Centrosome
FERM domain
Spindle midzone
Cell Biology
Actins
Cell biology
enzymes and coenzymes (carbohydrates)
Midbody
Protein Tyrosine Phosphatases
Cell Division
Rho Guanine Nucleotide Exchange Factors
Cytokinesis
HeLa Cells
Subjects
Details
- ISSN :
- 19394586 and 10591524
- Volume :
- 14
- Database :
- OpenAIRE
- Journal :
- Molecular Biology of the Cell
- Accession number :
- edsair.doi.dedup.....485eaec7a9995d37b6a43ab2678de7be