title: Phospho-regulation of DDA3 function in mitosis.
abstract: DDA3 is a microtubule-associated protein that controls chromosome congression and segregation by regulating the mitotic spindle. Depletion of DDA3 alters spindle structure, generates unaligned chromosomes at metaphase, and delays the mitotic progression. Through a mass spectrometry analysis, we found that DDA3 is phosphorylated on Ser225 during mitosis. Phosphorylation of this residue is important for the mitotic function of DDA3, as the phospho-mimicking DDA3-S225D variant, but not the nonphosphorable DDA3-S225A mutant, rescues the DDA3-knockdown phenotype. We conclude that the mitotic function of DDA3 is regulated by phosphorylation on the Ser225 residue.
authors.affiliation: Department of Biological Sciences, Stanford University, CA 94305-5020, USA.
authors.forename: Chang-Young
authors.initials: CY
authors.lastname: Jang
authors.forename: Judith A
authors.initials: JA
authors.lastname: Coppinger
authors.forename: John R
authors.initials: JR
authors.lastname: Yates
authors.forename: Guowei
authors.initials: G
authors.lastname: Fang
mesh_terms: D000595:Amino Acid Sequence; D023902:Chromosome Pairing; D006367:HeLa Cells; D006801:Humans; D008938:Mitosis; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation / Q000235:genetics; D012694:Serine / Q000235:genetics / Q000378:metabolism
chemical_list: C485740:PSRC1 protein, human; D010750:Phosphoproteins; D012694:Serine