Please use this identifier to cite or link to this item: https://doi.org/10.1083/jcb.144.1.71
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dc.titleRegulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p
dc.contributor.authorZeng, G.
dc.contributor.authorCai, M.
dc.date.accessioned2014-12-12T07:33:58Z
dc.date.available2014-12-12T07:33:58Z
dc.date.issued1999-01-11
dc.identifier.citationZeng, G., Cai, M. (1999-01-11). Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p. Journal of Cell Biology 144 (1) : 71-82. ScholarBank@NUS Repository. https://doi.org/10.1083/jcb.144.1.71
dc.identifier.issn00219525
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/115906
dc.description.abstractNormal actin cytoskeleton organization in budding yeast requires the function of the Pan1p/End3p complex. Mutations in 1 and END3 cause defects in the organization of actin cytoskeleton and endocytosis. By screening for mutations that can suppress the temperature sensitivity of a pan1 mutant (pan1-4), a novel serine/threonine kinase Prk1p is now identified as a new factor regulating the actin cytoskeleton organization in yeast. The suppression of pan1-4 by prk1 requires the presence of mutant Pan1p. Although viable, the prk1 mutant is unable to maintain an asymmetric distribution of the actin cytoskeleton at 37°C. Consistent with its role in the regulation of actin cytoskeleton, Prk1p localizes to the regions of cell growth and coincides with the polarized actin patches. Overexpression of the PRK1 gene in wild-type cells leads to lethality and actin cytoskeleton abnormalities similar to those exhibited by the pan1 and end3 mutants. In vitro phosphorylation assays demonstrate that Prk1p is able to phosphorylate regions of Pan1p containing the LxxQxTG repeats, including the region responsible for binding to End3p. Based on these findings, we propose that the Prk1 protein kinase regulates the actin cytoskeleton organization by modulating the activities of some actin cytoskeleton-related proteins such as Pan1p/End3p.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1083/jcb.144.1.71
dc.sourceScopus
dc.subjectActin cytoskeleton
dc.subjectCell polarity
dc.subjectEH domain
dc.subjectPhosphorylation
dc.subjectProtein kinase
dc.typeArticle
dc.contributor.departmentINSTITUTE OF MOLECULAR & CELL BIOLOGY
dc.description.doi10.1083/jcb.144.1.71
dc.description.sourcetitleJournal of Cell Biology
dc.description.volume144
dc.description.issue1
dc.description.page71-82
dc.description.codenJCLBA
dc.identifier.isiut000078084800008
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