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 K.; Matsumura, Fumio; Wei, Qize

doi:10.1074/jbc.m113.510388

Cited by 7 publications

(12 citation statements)

References 60 publications

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“…Aurora B and Plk1 are two mitotic kinases that play critical roles in the regulation of cytokinesis (27,28). Aurora B and Plk1 can promote MyoGEF activation and localization at the central spindle during cytokinesis by phosphorylating Myo-GEF at Thr-544 and Thr-574, respectively (31,32). Our findings in this study show that phosphorylation of the MyoGEF carboxyl-terminal region by aurora B relieves the intramolecular interaction between the DH domain and the carboxyl-terminal region of MyoGEF (Figs.…”

Section: Discussionsupporting

confidence: 57%

“…Depletion of Myo-GEF decreases RhoA/RhoC activation and suppresses breast cancer cell invasion (15). We also found that phosphorylation of MyoGEF at Thr-544 by aurora B creates a docking site for Plk1, thus leading to the binding of Plk1 to MyoGEF (31). In turn, Plk1 phosphorylates MyoGEF at Thr-574 (32).…”

Section: We Have Reported Previously That Nonmuscle Myosin Ii-interacmentioning

confidence: 76%

“…This finding suggested that the MyoGEF carboxyl-terminal region could bind to MyoGEF and inhibit its ability to activate RhoA. lation of MyoGEF at Thr-544 creates a docking site for Plk1 to bind MyoGEF (31). In turn, Plk1 can phosphorylate MyoGEF at Thr-574 (32).…”

Section: Exogenous Expression Of the Myogef Carboxyl-terminal Region mentioning

confidence: 95%

“…It has been shown that the carboxyl-terminal region of MyoGEF can interact with centrosome/spindle-associated protein (CSPP), ezrin, and GIPC1 (46,47,58). Aurora B and Plk1 can phosphorylate the carboxyl-terminal region of MyoGEF (31,32). Therefore, exogenous expression of the MyoGEF carboxylterminal region in transfected cells could potentially cause cell phenotypes through interference with protein-protein interactions and phosphorylation involving the carboxyl-terminal region of MyoGEF.…”

Section: Discussionmentioning

confidence: 99%

“…We have reported previously that MyoGEF plays an important role in the regulation of cytokinesis and breast cancer cell invasion (15,24,31,32,46,47). MyoGEF is highly expressed in invasive breast cancer cells and tissues (15).…”

Section: We Have Reported Previously That Nonmuscle Myosin Ii-interacmentioning

confidence: 99%

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Intramolecular Interactions between the Dbl Homology (DH) Domain and the Carboxyl-terminal region of Myosin II-interacting Guanine Nucleotide Exchange Factor (MyoGEF) Act as an Autoinhibitory Mechanism for the Regulation of MyoGEF Functions

Jiao

et al. 2014

Journal of Biological Chemistry

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Background: MyoGEF is implicated in regulating cytokinesis and breast cancer cell invasion. Results: Binding of the MyoGEF carboxyl-terminal region to its DH domain suppresses breast cancer cell invasion and interferes with cytokinesis. Conclusion: Intramolecular interactions of MyoGEF act as an autoinhibitory mechanism to regulate MyoGEF functions. Significance: Autoinhibitory intramolecular interactions of MyoGEF serve as a control point to regulate cytokinesis and breast cancer cell invasion.

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Section: Discussionsupporting

confidence: 57%

Section: We Have Reported Previously That Nonmuscle Myosin Ii-interacmentioning

confidence: 76%

Section: Exogenous Expression Of the Myogef Carboxyl-terminal Region mentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Section: We Have Reported Previously That Nonmuscle Myosin Ii-interacmentioning

confidence: 99%

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Intramolecular Interactions between the Dbl Homology (DH) Domain and the Carboxyl-terminal region of Myosin II-interacting Guanine Nucleotide Exchange Factor (MyoGEF) Act as an Autoinhibitory Mechanism for the Regulation of MyoGEF Functions

Jiao

et al. 2014

Journal of Biological Chemistry

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Controlling the switches: Rho GTPase regulation during animal cell mitosis

Zuo

Frost

2014

Cellular Signalling

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Animal cell division is a fundamental process that requires complex changes in cytoskeletal organization and function. Aberrant cell division often has disastrous consequences for the cell and can lead to cell senescence, neoplastic transformation or death. As important regulators of the actin cytoskeleton, Rho GTPases play major roles in regulating many aspects of mitosis and cytokinesis. These include centrosome duplication and separation, generation of cortical rigidity, microtubule-kinetochore stabilization, cleavage furrow formation, contractile ring formation and constriction, and abscission. The ability of Rho proteins to function as regulators of cell division depends on their ability to cycle between their active, GTP-bound and inactive, GDP-bound states. However, Rho proteins are inherently inefficient at fulfilling this cycle and require the actions of regulatory proteins that enhance GTP binding (RhoGEFs), stimulate GTPase activity (RhoGAPs), and sequester inactive Rho proteins in the cytosol (RhoGDIs). The roles of these regulatory proteins in controlling cell division are an area of active investigation. In this review we will delineate the current state of knowledge of how specific RhoGEFs, RhoGAPs and RhoGDIs control mitosis and cytokinesis, and highlight the mechanisms by which their functions are controlled.

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Regulating Rho GTPases and their regulators

Hodge

Ridley²

2016

Nat Rev Mol Cell Biol

734

657

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Rho GTPases regulate cytoskeletal and cell adhesion dynamics and thereby coordinate a wide range of cellular processes, including cell migration, cell polarity and cell cycle progression. Most Rho GTPases cycle between a GTP-bound active conformation and a GDP-bound inactive conformation to regulate their ability to activate effector proteins and to elicit cellular responses. However, it has become apparent that Rho GTPases are regulated by post-translational modifications and the formation of specific protein complexes, in addition to GTP-GDP cycling. The canonical regulators of Rho GTPases - guanine nucleotide exchange factors, GTPase-activating proteins and guanine nucleotide dissociation inhibitors - are regulated similarly, creating a complex network of interactions to determine the precise spatiotemporal activation of Rho GTPases.

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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

Cited by 7 publications

References 60 publications

Intramolecular Interactions between the Dbl Homology (DH) Domain and the Carboxyl-terminal region of Myosin II-interacting Guanine Nucleotide Exchange Factor (MyoGEF) Act as an Autoinhibitory Mechanism for the Regulation of MyoGEF Functions

Intramolecular Interactions between the Dbl Homology (DH) Domain and the Carboxyl-terminal region of Myosin II-interacting Guanine Nucleotide Exchange Factor (MyoGEF) Act as an Autoinhibitory Mechanism for the Regulation of MyoGEF Functions

Controlling the switches: Rho GTPase regulation during animal cell mitosis

Regulating Rho GTPases and their regulators

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