ArticlePloS one2011
Roles of the DYRK kinase Pom2 in cytokinesis, mitochondrial morphology, and sporulation in fission yeast.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Protocol for assessing protein expression levels and localization during fission yeast cytokinesis.STAR protocols · 2026Article
- Sporulation: A response to starvation in the fission yeast Schizosaccharomyces pombe.MicrobiologyOpen · 2022Review
- Roles of Mso1 and the SM protein Sec1 in efficient vesicle fusion during fission yeast cytokinesis.Molecular biology of the cell · 2020Article
- Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis.Molecular biology of the cell · 2018Article
- Roles of the TRAPP-II Complex and the Exocyst in Membrane Deposition during Fission Yeast Cytokinesis.PLoS biology · 2016Article
- The novel proteins Rng8 and Rng9 regulate the myosin-V Myo51 during fission yeast cytokinesis.The Journal of cell biology · 2014Article
- Cooperation between Rho-GEF Gef2 and its binding partner Nod1 in the regulation of fission yeast cytokinesis.Molecular biology of the cell · 2013Article
- Characterization of Mid1 domains for targeting and scaffolding in fission yeast cytokinesis.Journal of cell science · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.