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 pom2Δ 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.
Highlights
Dual-specificity tyrosine-phosphorylation regulated kinases (DYRKs), a family of evolutionarily conserved protein kinases, are known for their capability of autophosphorylating tyrosine residues in their own activation loops and phosphorylating serine/ threonine residues on exogenous substrates [1,2,3]
Based on the homology within the kinase domain, the DYRK family can be grouped into three subfamilies: DYRK kinases, homeodomaininteracting protein kinases, and pre-mRNA processing protein 4 kinases [4]
Our results show that Pom2 localizes to the division site during cytokinesis and mitochondria throughout the cell cycle
Summary
Dual-specificity tyrosine-phosphorylation regulated kinases (DYRKs), a family of evolutionarily conserved protein kinases, are known for their capability of autophosphorylating tyrosine residues in their own activation loops and phosphorylating serine/ threonine residues on exogenous substrates [1,2,3]. Based on the homology within the kinase domain, the DYRK family can be grouped into three subfamilies: DYRK kinases, homeodomaininteracting protein kinases, and pre-mRNA processing protein 4 kinases [4]. The functions of several DYRK kinases in yeasts, Caenorhabditis elegans, Drosophila, and mammals have been unraveled, and accumulating evidence suggests that DYRK kinases function in cell proliferation and cell differentiation [5]. Yak (the founding member of the DYRK family), on the other hand, is a growth inhibitor by negatively regulating the Ras/ cAMP and TOR (target of rapamycin) pathway under nutritional stress [16,17,18].
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