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Article

Fission yeast Pak1 phosphorylates anillin-like Mid1 for spatial control of cytokinesis.

The Journal of cell biology - 3 Aug 2020

Magliozzi Joseph O, Sears Jack, Cressey Lauren, Brady Marielle, Opalko Hannah E, Kettenbach Arminja N, Moseley James B

Abstract excerpt

Protein kinases direct polarized growth by regulating the cytoskeleton in time and space and could play similar roles in cell division. We found that the Cdc42-activated polarity kinase Pak1 colocalizes with the assembling contractile actomyosin ring (CAR) and remains at the division site during septation. Mutations in pak1 led to defects in CAR assembly and genetic interactions with cytokinesis mutants. Through...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 32421151
DOI: 10.1083/jcb.201908017
PMCID: PMC7401808

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Fission yeast Pak1 phosphorylates anillin-like Mid1 for spatial control of cytokinesis.PMID 32421151Read ↗

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Schizosaccharomyces pombe Pak-related protein, Pak1p/Orb2p, phosphorylates myosin regulatory light chain to inhibit cytokinesis.Semantic proximity Read ↗

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Role of the protein kinase Kin1 and nuclear centering in actomyosin ring formation in fission yeast.Semantic proximity Read ↗

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C-terminal anchoring of mid1p to membranes stabilizes cytokinetic ring position in early mitosis in fission yeast.Semantic proximity Read ↗

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