title: Myosin-II reorganization during mitosis is controlled temporally by its dephosphorylation and spatially by Mid1 in fission yeast.
abstract: Cytokinesis in many eukaryotes requires an actomyosin contractile ring. Here, we show that in fission yeast the myosin-II heavy chain Myo2 initially accumulates at the division site via its COOH-terminal 134 amino acids independently of F-actin. The COOH-terminal region can access to the division site at early G2, whereas intact Myo2 does so at early mitosis. Ser1444 in the Myo2 COOH-terminal region is a phosphorylation site that is dephosphorylated during early mitosis. Myo2 S1444A prematurely accumulates at the future division site and promotes formation of an F-actin ring even during interphase. The accumulation of Myo2 requires the anillin homologue Mid1 that functions in proper ring placement. Myo2 interacts with Mid1 in cell lysates, and this interaction is inhibited by an S1444D mutation in Myo2. Our results suggest that dephosphorylation of Myo2 liberates the COOH-terminal region from an intramolecular inhibition. Subsequently, dephosphorylated Myo2 is anchored by Mid1 at the medial cortex and promotes the ring assembly in cooperation with F-actin.
authors.affiliation: Division of Biology, Department of Life Sciences, Graduate School of Arts and Science, University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902, Japan.
authors.forename: Fumio
authors.initials: F
authors.lastname: Motegi
authors.forename: Mithilesh
authors.initials: M
authors.lastname: Mishra
authors.forename: Mohan K
authors.initials: MK
authors.lastname: Balasubramanian
authors.forename: Issei
authors.initials: I
authors.lastname: Mabuchi
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000096:biosynthesis; D000595:Amino Acid Sequence / Q000502:physiology; D016195:G2 Phase / Q000502:physiology; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D008938:Mitosis / Q000502:physiology*; D009154:Mutation / Q000235:genetics; D018995:Myosin Heavy Chains / Q000235:genetics / Q000378:metabolism; D024462:Myosin Type II / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D017434:Protein Structure, Tertiary / Q000502:physiology; D012568:Schizosaccharomyces / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D000199:Actins; C434211:MYO2 protein, S pombe; D008562:Membrane Glycoproteins; C489694:Mid1 protein, S pombe; D029702:Schizosaccharomyces pombe Proteins; C405644:YAM8 protein, S pombe; D024462:Myosin Type II; D018995:Myosin Heavy Chains