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Elife. 2017 Sep 15;6. pii: e28865. doi: 10.7554/eLife.28865.

Nanoscale architecture of the Schizosaccharomyces pombe contractile ring.

Author information

1
Department of Cell and Developmental Biology, Vanderbilt University, Nashville, United States.
2
Department of Biomedical Informatics, Vanderbilt University Medical Center, Nashville, United States.
3
Stowers Institute for Medical Research, Kansas City, United States.
4
Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, United States.

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 influence cell division. Farthest from the membrane (160-350 nm) we find F-actin, the motor domains of myosins, and a major F-actin crosslinker. Circumferentially within the ring, multiple proteins proximal to the membrane form clusters of different sizes, while components farther from the membrane are uniformly distributed. This comprehensive organizational map provides a framework for understanding contractile ring function.

KEYWORDS:

S. pombe; actin; cell biology; cytokinesis; super-resolution microscopy

PMID:
28914606
PMCID:
PMC5779233
DOI:
10.7554/eLife.28865
[Indexed for MEDLINE]
Free PMC Article

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