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Curr Biol. 2010 Aug 10;20(15):R649-54. doi: 10.1016/j.cub.2010.07.004.

Cytoskeletal cross-linking and bundling in motor-independent contraction.

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Johns Hopkins University, Department of Mechanical Engineering, Institute for NanoBioTechnology, Baltimore, MD, USA.


Eukaryotic and prokaryotic cells use cytoskeletal proteins to regulate and modify cell shape. During cytokinesis or eukaryotic cell crawling, contractile forces are generated inside the cell to constrict the division site or to haul the rear of the cell forward, respectively. In many cases, these forces have been attributed to the activity of molecular motors, such as myosin II, which, by pulling on actin filaments, can produce contraction of the actin cytoskeleton. However, prokaryotic division is driven by the tubulin-like protein FtsZ and does not seem to require additional molecular motors to constrict the division site. Likewise, Dictyostelium discoideum and Saccharomyces cerevisiae can perform cytokinesis under motor-free conditions. In addition, many crawling cells can translocate when myosin is inhibited or absent. In this review, we point out another force-generation mechanism that can play a significant role in driving these processes in eukaryotes and prokaryotes. This mechanism is mediated by cross-linking and bundling proteins that form effective interactions between cytoskeletal filaments. Some recent studies in this area are reviewed and the physical underpinnings of this force-generation mechanism are explained.

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