Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.biocel.2004.03.010
DC FieldValue
dc.titlePrk1p
dc.contributor.authorZeng, G.
dc.contributor.authorCai, M.
dc.date.accessioned2014-12-01T06:58:46Z
dc.date.available2014-12-01T06:58:46Z
dc.date.issued2005-01
dc.identifier.citationZeng, G., Cai, M. (2005-01). Prk1p. International Journal of Biochemistry and Cell Biology 37 (1) : 48-53. ScholarBank@NUS Repository. https://doi.org/10.1016/j.biocel.2004.03.010
dc.identifier.issn13572725
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/113812
dc.description.abstractThe protein kinase Prk1p (standing for p53 regulating kinase 1) of the yeast Saccharomyces cerevisiae is the prototype of a kinase family identified recently as important regulators of the actin cytoskeleton and endocytosis. These kinases all have a highly homologous serine/threonine kinase domain in their N-terminal region but share no significant homology in other regions. Prk1p also contains a proline-rich motif near its C-terminus that is required for the proper subcellular localization of the protein. The kinase activity of Prk1p has been confirmed by both in vitro and in vivo studies and shown to be essential for the protein's function. To date, several proteins that play essential roles in actin cytoskeleton organization and endocytosis have been identified as the regulatory targets of Prk1p. Phosphorylation on the [L/I/V/N]xx[Q/N/T/S]xTG motifs by Prk1p results in a down-regulation of the functions of these target proteins. The observation that many yeast proteins involved in the actin cytoskeleton organization and endocytosis contain the Prk1p phosphorylation motifs has led to the hypothesis that the Prk1p family of kinases are possibly the general regulators of the actin cytoskeleton and endocytosis in yeast. © 2004 Elsevier Ltd. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.biocel.2004.03.010
dc.sourceScopus
dc.subjectActin cytoskeleton
dc.subjectEndocytosis
dc.subjectPhosphorylation
dc.subjectPrk1p kinase
dc.typeReview
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1016/j.biocel.2004.03.010
dc.description.sourcetitleInternational Journal of Biochemistry and Cell Biology
dc.description.volume37
dc.description.issue1
dc.description.page48-53
dc.description.codenIJBBF
dc.identifier.isiut000224605800008
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