Nanoscale architecture of the Schizosaccharomyces pombe contractile ring
- Vanderbilt University, United States
- Vanderbilt University Medical Center, United States
- Stowers Institute for Medical Research, United States
- Johns Hopkins University School of Medicine, United States
- Cited 25
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Abstract
The contractile ring is a complex molecular apparatus important for dividing many eukaryotic cells. Despite knowledge of its composition, the molecular architecture of the ring is not known. Here we applied super-resolution microscopy and FRET to determine the nanoscale spatial organization of Schizosaccharomyces pombe contractile ring components relative to the plasma membrane. As in other membrane-tethered actin structures, contractile ring proteins are stratified relative to the membrane. The lowest layer (0-80 nm) contains membrane-binding scaffolds, formin, and the myosin-II tail. An intermediate zone (80-160 nm) consists of a network of cytokinesis accessory proteins and signaling components that influence cell division. Most interior from the membrane (160-400 nm) is F-actin, myosin motor domains, and an F-actin crosslinker. Circumferentially within the ring, multiple proximal membrane proteins form different sized clusters, while components farther from the membrane are uniformly distributed. This comprehensive organizational map provides a framework for understanding contractile ring function.
Article and author information
Author details
Funding
National Institutes of Health (Research grant)
- Kathleen Gould
American Heart Association (Graduate Student Fellowship)
- Nathan A McDonald
National Institutes of Health (Research grant)
- Rong Li
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Reviewing Editor
- Mohan K Balasubramanian, University of Warwick, United Kingdom
Publication history
- Received: May 22, 2017
- Accepted: September 14, 2017
- Accepted Manuscript published: September 15, 2017 (version 1)
- Version of Record published: September 26, 2017 (version 2)
Copyright
© 2017, McDonald et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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