Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/108638
DC FieldValue
dc.titleMyosin light chain kinases: Division of work in cell migration
dc.contributor.authorTan, I.
dc.contributor.authorLeung, T.
dc.date.accessioned2014-11-25T09:48:32Z
dc.date.available2014-11-25T09:48:32Z
dc.date.issued2009-07
dc.identifier.citationTan, I.,Leung, T. (2009-07). Myosin light chain kinases: Division of work in cell migration. Cell Adhesion and Migration 3 (3) : 256-258. ScholarBank@NUS Repository.
dc.identifier.issn19336918
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/108638
dc.description.abstractCell motility is a highly coordinated multistep process. Uncovering the mechanism of myosin II (MYO2) activation responsible for the contractility underlying cell protrusion and retraction provides clues on how these complementary activities are coordinated. Several protein kinases have been shown to activate MYO2 by phosphorylating the associated myosin light chain (MLC). Recent work suggests that these MLC kinases are strategically localized to various cellular regions during cell migration in a polarized manner. This localization of the kinases together with their specificity in MLC phosphorylation, their distinct enzymatic properties and the distribution of the myosin isoforms generate the specific contractile activities that separately promote the cell protrusion or retraction essential for cell motility. ©2009 Landes Bioscience.
dc.sourceScopus
dc.subjectCell migration
dc.subjectMLCK
dc.subjectMRCK
dc.subjectMyosin
dc.subjectPhosphorylation
dc.subjectROK
dc.typeOthers
dc.contributor.departmentANATOMY
dc.description.sourcetitleCell Adhesion and Migration
dc.description.volume3
dc.description.issue3
dc.description.page256-258
dc.identifier.isiutNOT_IN_WOS
Appears in Collections:Staff Publications

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