title: Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p.
abstract: Normal actin cytoskeleton organization in budding yeast requires the function of the Pan1p/ End3p complex. Mutations in PAN1 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 degreesC. 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.
authors.affiliation: Institute of Molecular and Cell Biology, National University of Singapore, Singapore 117609.
authors.forename: G
authors.initials: G
authors.lastname: Zeng
authors.forename: M
authors.initials: M
authors.lastname: Cai
mesh_terms: D000199:Actins / Q000378:metabolism*; D000595:Amino Acid Sequence; D002455:Cell Division; D016764:Cell Polarity; D003599:Cytoskeleton / Q000502:physiology*; D005656:Fungal Proteins; D015870:Gene Expression; D008969:Molecular Sequence Data; D016296:Mutagenesis; D010766:Phosphorylation; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D020794:Receptor Protein-Tyrosine Kinases / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D029702:Schizosaccharomyces pombe Proteins; D017386:Sequence Homology, Amino Acid
chemical_list: D000199:Actins; D005656:Fungal Proteins; D029702:Schizosaccharomyces pombe Proteins; D011494:Protein Kinases; C061570:protein kinase N; C087019:ran1 protein, S pombe; D020794:Receptor Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D011493:Protein Kinase C