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Phosphorylation of myosin II-interacting guanine nucleotide exchange factor (MyoGEF) at threonine 544 by aurora B kinase promotes the binding of polo-like kinase 1 to MyoGEF.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2014 Mar 07; Vol. 289 (10), pp. 7142-7150. Date of Electronic Publication: 2014 Jan 30. - Publication Year :
- 2014
-
Abstract
- We previously reported that phosphorylation of myosin II-interacting guanine nucleotide exchange factor (MyoGEF) by polo-like kinase 1 (Plk1) promotes the localization of MyoGEF to the central spindle and increases MyoGEF activity toward RhoA during mitosis. In this study we report that aurora B-mediated phosphorylation of MyoGEF at Thr-544 creates a docking site for Plk1, leading to the localization and activation of MyoGEF at the central spindle. In vitro kinase assays show that aurora B can phosphorylate MyoGEF. T544A mutation drastically decreases aurora B-mediated phosphorylation of MyoGEF in vitro and in transfected HeLa cells. Coimmunoprecipitation and in vitro pulldown assays reveal that phosphorylation of MyoGEF at Thr-544 enhances the binding of Plk1 to MyoGEF. Immunofluorescence analysis shows that aurora B colocalizes with MyoGEF at the central spindle and midbody during cytokinesis. Suppression of aurora B activity by an aurora B inhibitor disrupts the localization of MyoGEF to the central spindle. In addition, T544A mutation interferes with the localization of MyoGEF to the cleavage furrow and decreases MyoGEF activity toward RhoA during mitosis. Taken together, our results suggest that aurora B coordinates with Plk1 to regulate MyoGEF activation and localization, thus contributing to the regulation of cytokinesis.
- Subjects :
- Guanine Nucleotide Exchange Factors genetics
HeLa Cells
Humans
Immunoprecipitation
Mitosis
Phosphorylation
Protein Binding
Spindle Apparatus metabolism
Threonine genetics
Polo-Like Kinase 1
Aurora Kinase B metabolism
Cell Cycle Proteins metabolism
Cytokinesis
Guanine Nucleotide Exchange Factors metabolism
Protein Serine-Threonine Kinases metabolism
Proto-Oncogene Proteins metabolism
Threonine metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 289
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 24482237
- Full Text :
- https://doi.org/10.1074/jbc.M113.510388