roles of the dyrk kinase pom2 in cytokinesis, mitochondrial morphology, and sporulation in fission yeast角色的dyrk激酶pom2在胞质分裂,线粒体形态、和裂殖酵母孢子形成.pdfVIP
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roles of the dyrk kinase pom2 in cytokinesis, mitochondrial morphology, and sporulation in fission yeast角色的dyrk激酶pom2在胞质分裂,线粒体形态、和裂殖酵母孢子形成
Roles of the DYRK Kinase Pom2 in Cytokinesis,
Mitochondrial Morphology, and Sporulation in Fission
Yeast
Pengcheng Wu1.¤, Ran Zhao1., Yanfang Ye1,2, Jian-Qiu Wu1,2*
1 Department of Molecular Genetics, The Ohio State University, Columbus, Ohio, United States of America, 2 Department of Molecular and Cellular Biochemistry, The Ohio
State University, Columbus, Ohio, United States of America
Abstract
Pom2 is predicted to be a dual-specificity tyrosine-phosphorylation regulated kinase (DYRK) related to Pom1 in
Schizosaccharomyces pombe. DYRKs share a kinase domain capable of catalyzing autophosphorylation on tyrosine and
exogenous phosphorylation on serine/threonine residues. Here we show that Pom2 is functionally different from the well-
characterized Pom1, although they share 55% identity in the kinase domain and the Pom2 kinase domain functionally
complements that of Pom1. Pom2 localizes to mitochondria throughout the cell cycle and to the contractile ring during late
stages of cytokinesis. Overexpression but not deletion of pom2 results in severe defects in cytokinesis, indicating that Pom2
might share an overlapping function with other proteins in regulating cytokinesis. Gain and loss of function analyses reveal
that Pom2 is required for maintaining mitochondrial morphology independently of microtubules. Intriguingly, most meiotic
pom2D cells form aberrant asci with meiotic and/or forespore membrane formation defects. Taken together, Pom2 is a
novel DYRK kinase involved in regulating cytokinesis, mitochondrial morphology, meiosis, and sporulation in fission yeast.
Citation: Wu P, Zhao R, Ye Y, Wu J-Q (2011) Roles of the DYRK Kinase Pom2 in Cytokinesis, Mitochondrial Morphology, and Sporulation in Fission Yeast. PLoS
ONE 6(12): e28000. doi:10.1371/journal.pone.0028000
Editor: Daniel Lew, Duke Univers
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