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

Di Wu; Michael Asiedu; Fumio Matsumura; Qize Wei

doi:10.1074/jbc.M113.510388

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

Di Wu, Michael Asiedu, Fumio Matsumura, Qize Wei

School of Arts and Sciences, Molecular Biology & Biochemistry

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Background: Aurora B kinase (aurora B) and polo-like kinase 1 (Plk1) are critical regulators of cytokinesis. Results: Phosphorylation of MyoGEF at Thr-544 by aurora B promotes the binding of Plk1 to MyoGEF. Conclusion: Phosphorylation of MyoGEF by aurora B creates a docking site for Plk1. Significance: Coordinated regulation of MyoGEF localization and activation by aurora B and Plk1 contributes to the regulation of cytokinesis.

Original language	English (US)
Pages (from-to)	7142-7150
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	289
Issue number	10
DOIs	https://doi.org/10.1074/jbc.M113.510388
State	Published - Mar 7 2014

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.510388

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title = "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",

abstract = "Background: Aurora B kinase (aurora B) and polo-like kinase 1 (Plk1) are critical regulators of cytokinesis. Results: Phosphorylation of MyoGEF at Thr-544 by aurora B promotes the binding of Plk1 to MyoGEF. Conclusion: Phosphorylation of MyoGEF by aurora B creates a docking site for Plk1. Significance: Coordinated regulation of MyoGEF localization and activation by aurora B and Plk1 contributes to the regulation of cytokinesis.",

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doi = "10.1074/jbc.M113.510388",

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journal = "Journal of Biological Chemistry",

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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. / Wu, Di; Asiedu, Michael; Matsumura, Fumio et al.
In: Journal of Biological Chemistry, Vol. 289, No. 10, 07.03.2014, p. 7142-7150.

Research output: Contribution to journal › Article › peer-review

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T1 - 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

AU - Wu, Di

AU - Asiedu, Michael

AU - Matsumura, Fumio

AU - Wei, Qize

PY - 2014/3/7

Y1 - 2014/3/7

N2 - Background: Aurora B kinase (aurora B) and polo-like kinase 1 (Plk1) are critical regulators of cytokinesis. Results: Phosphorylation of MyoGEF at Thr-544 by aurora B promotes the binding of Plk1 to MyoGEF. Conclusion: Phosphorylation of MyoGEF by aurora B creates a docking site for Plk1. Significance: Coordinated regulation of MyoGEF localization and activation by aurora B and Plk1 contributes to the regulation of cytokinesis.

AB - Background: Aurora B kinase (aurora B) and polo-like kinase 1 (Plk1) are critical regulators of cytokinesis. Results: Phosphorylation of MyoGEF at Thr-544 by aurora B promotes the binding of Plk1 to MyoGEF. Conclusion: Phosphorylation of MyoGEF by aurora B creates a docking site for Plk1. Significance: Coordinated regulation of MyoGEF localization and activation by aurora B and Plk1 contributes to the regulation of cytokinesis.

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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

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