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Cooperation between Paxillin-like Protein Pxl1 and Glucan Synthase Bgs1 Is Essential for Actomyosin Ring Stability and Septum Formation in Fission Yeast
Cytokinesis requires assembly of an actomyosin ring adjacent to the plasma membrane, which upon contraction pulls the membrane to form a cleavage furrow. In fungi ring closure is coordinated with the synthesis of a cell wall septum. Knowledge about the molecules anchoring the ring to the membrane is very limited. We have found that fission yeast paxillin, located at the ring, and Bgs1, the enzyme responsible for primary septum formation, located at the membrane, cooperate during cytokinesis. Both are required to anchor the ring to the membrane and to maintain it during cytokinesis. Moreover, both proteins cooperate to form the septum. Accordingly, paxillin is essential when Bgs1 is depleted. When both proteins are missing, the contractile ring forms but the lateral cell wall overgrows inwards without a defined cleavage furrow and septum formation. During cytokinesis there is an increase of paxillin which depends on the SH3 domain of the F-BAR protein Cdc15. Consequently the absence of this domain mimics the phenotype of paxillin absence in Bgs1-depleted cells. Interestingly, a decreased function of both Cdc15 and paxillin uncouples the septum synthesis from the ring contraction, indicating an essential cooperation between these proteins and Bgs1 for proper cytokinesis.
Vyšlo v časopise: Cooperation between Paxillin-like Protein Pxl1 and Glucan Synthase Bgs1 Is Essential for Actomyosin Ring Stability and Septum Formation in Fission Yeast. PLoS Genet 11(7): e32767. doi:10.1371/journal.pgen.1005358
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1005358Souhrn
Cytokinesis requires assembly of an actomyosin ring adjacent to the plasma membrane, which upon contraction pulls the membrane to form a cleavage furrow. In fungi ring closure is coordinated with the synthesis of a cell wall septum. Knowledge about the molecules anchoring the ring to the membrane is very limited. We have found that fission yeast paxillin, located at the ring, and Bgs1, the enzyme responsible for primary septum formation, located at the membrane, cooperate during cytokinesis. Both are required to anchor the ring to the membrane and to maintain it during cytokinesis. Moreover, both proteins cooperate to form the septum. Accordingly, paxillin is essential when Bgs1 is depleted. When both proteins are missing, the contractile ring forms but the lateral cell wall overgrows inwards without a defined cleavage furrow and septum formation. During cytokinesis there is an increase of paxillin which depends on the SH3 domain of the F-BAR protein Cdc15. Consequently the absence of this domain mimics the phenotype of paxillin absence in Bgs1-depleted cells. Interestingly, a decreased function of both Cdc15 and paxillin uncouples the septum synthesis from the ring contraction, indicating an essential cooperation between these proteins and Bgs1 for proper cytokinesis.
Zdroje
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