Cell
Altered phosphorylation and activation of PP60c-src during fibroblast mitosis
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Cited by (227)
The tyrosine kinase v-Src causes mitotic slippage by phosphorylating an inhibitory tyrosine residue of Cdk1
2018, Journal of Biological ChemistryCitation Excerpt :The Src-family kinases play some roles in cell division. At mitotic entry, the kinase activities of the Src-family kinases increase through dephosphorylation of the C-terminal inhibitory tyrosine residue (8–12). Inhibition of the Src-family kinases, which is caused by microinjection of anti-Src antibodies or treatment with inhibitors, prevents mitotic entry or causes mitotic defects (13–17).
V-Src causes delocalization of Mklp1, Aurora B, and INCENP from the spindle midzone during cytokinesis failure
2013, Experimental Cell Researchc-Src but not Fyn promotes proper spindle orientation in early prometaphase
2012, Journal of Biological ChemistryCitation Excerpt :Furthermore, the specific Src family kinase inhibitor PP2 (18) inhibits cytokinesis, which is also prevented by the MEK inhibitor U0126 (15), suggesting a role of the Src/MEK/ERK pathway in regulation of cytokinesis. The kinase activities of SFKs are up-regulated upon mitotic entry through Cdk1-induced phosphorylation of the unique domain of SFKs, which promotes dephosphorylation of the C-terminal inhibitory tyrosine residue (19–23). Although SFKs are involved in the regulation of mitotic entry and cytokinesis, the precise roles of SFKs in cell division are not fully understood.
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Current address: Amala Cancer Research Institute, Amala Nagar, Trichur 680553, Kerala, India.