title: CDK phosphorylates the polarisome scaffold Spa2 to maintain its localization at the site of cell growth.
abstract: Polarisome is a protein complex that plays an important role in polarized growth in fungi by assembling actin cables towards the site of cell growth. For proper morphogenesis, the polarisome must localize to the right place at the right time. However, the mechanisms that control polarisome localization remain poorly understood. In this study, using the polymorphic fungus Candida albicans as a model, we have discovered that the cyclin-dependent kinase (CDK) Cdc28 phosphorylates the polarisome scaffold protein Spa2 to govern polarisome localization during both yeast and hyphal growth. In a yeast cell cycle, Cdc28-Clb2 phosphorylates Spa2 and controls the timing of polarisome translocation from the bud tip to the bud neck. And during hyphal development, Cdc28-Clb2 and the hyphal-specific Cdc28-Hgc1 cooperate to enhance Spa2 phosphorylation to maintain the polarisome at the hyphal tip. Blocking the CDK phosphorylation causes premature tip-to-neck translocation of Spa2 during yeast growth and inappropriate septal localization of Spa2 in hyphae and abnormal hyphal morphology under certain inducing conditions. Together, our results generate new insights into the mechanisms by which fungi regulate polarisome localization in the control of polarized growth.
authors.affiliation: Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research, Singapore.|Faculty of Health Sciences, University of Macau, Macau, China.
authors.forename: Haitao
authors.initials: H
authors.lastname: Wang
authors.affiliation: Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research, Singapore.
authors.forename: Zhen-Xing
authors.initials: ZX
authors.lastname: Huang
authors.affiliation: Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research, Singapore.
authors.forename: Jie Ying
authors.initials: JY
authors.lastname: Au Yong
authors.affiliation: Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research, Singapore.
authors.forename: Hao
authors.initials: H
authors.lastname: Zou
authors.affiliation: Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research, Singapore.
authors.forename: Guisheng
authors.initials: G
authors.lastname: Zeng
authors.affiliation: Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research, Singapore.
authors.forename: Jiaxin
authors.initials: J
authors.lastname: Gao
authors.affiliation: Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research, Singapore.
authors.forename: Yanming
authors.initials: Y
authors.lastname: Wang
authors.affiliation: Faculty of Health Sciences, University of Macau, Macau, China.
authors.forename: Ada Hang-Heng
authors.initials: AH
authors.lastname: Wong
authors.affiliation: Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research, Singapore.|Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore.
authors.forename: Yue
authors.initials: Y
authors.lastname: Wang
mesh_terms: D017489:CDC28 Protein Kinase, S cerevisiae / Q000378:metabolism*; D002176:Candida albicans / Q000254:growth & development / Q000378:metabolism; D002453:Cell Cycle / Q000235:genetics; D016764:Cell Polarity / Q000235:genetics / Q000502:physiology*; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal / Q000235:genetics; D025301:Hyphae / Q000254:growth & development / Q000378:metabolism; D010766:Phosphorylation; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
chemical_list: D003598:Cytoskeletal Proteins; D005656:Fungal Proteins; C065889:SPA2 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D017489:CDC28 Protein Kinase, S cerevisiae