Phosphoinositide-mediated ring anchoring resists perpendicular forces to promote medial cytokinesis.
Chloe E SniderAlaina H WilletJun-Song ChenGöker ArpağMarija ZanicKathleen L GouldPublished in: The Journal of cell biology (2017)
Many eukaryotic cells divide by assembling and constricting an actin- and myosin-based contractile ring (CR) that is physically linked to the plasma membrane (PM). In this study, we report that Schizosaccharomyces pombe cells lacking efr3, which encodes a conserved PM scaffold for the phosphatidylinositol-4 kinase Stt4, build CRs that can slide away from the cell middle during anaphase in a myosin V-dependent manner. The Efr3-dependent CR-anchoring mechanism is distinct from previously reported pathways dependent on the Fes/CIP4 homology Bin-Amphiphysin-Rvs167 (F-BAR) protein Cdc15 and paxillin Pxl1. In efr3Δ, the concentrations of several membrane-binding proteins were reduced in the CR and/or on the PM. Our results suggest that proper PM lipid composition is important to stabilize the central position of the CR and resist myosin V-based forces to promote the fidelity of cell division.
Keyphrases
- particulate matter
- air pollution
- induced apoptosis
- binding protein
- polycyclic aromatic hydrocarbons
- heavy metals
- single cell
- cell cycle arrest
- cell therapy
- water soluble
- endoplasmic reticulum stress
- signaling pathway
- cell death
- cell cycle
- skeletal muscle
- risk assessment
- oxidative stress
- protein kinase
- cell proliferation
- amino acid
- smooth muscle