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Nanoscale architecture of the Schizosaccharomyces pombe contractile ring.


ABSTRACT: The contractile ring is a complex molecular apparatus which physically divides many eukaryotic cells. Despite knowledge of its protein composition, the molecular architecture of the ring is not known. Here we have applied super-resolution microscopy and FRET to determine the nanoscale spatial organization of Schizosaccharomyces pombe contractile ring components relative to the plasma membrane. Similar to other membrane-tethered actin structures, we find proteins localize in specific layers relative to the membrane. The most membrane-proximal layer (0-80 nm) is composed of membrane-binding scaffolds, formin, and the tail of the essential myosin-II. An intermediate layer (80-160 nm) consists of a network of cytokinesis accessory proteins as well as multiple signaling components which influen

SUBMITTER: McDonald NA 

PROVIDER: S-EPMC5779233 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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