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Bioessays. 2005 Jan;27(1):5-8.

Reining in cytokinesis with a septin corral.

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  • 1Biology Department, Rensselaer Polytechnic Institute, 110 8th St. Troy, NY 12180, USA. fingef@rpi.edu

Abstract

Septins are a family of conserved GTP-binding proteins that function in cytokinesis in fungi and animals. In budding yeast, septins form scaffolds for assembly of the actomyosin contractile ring at the cleavage plane, a role that does not appear to be conserved in other organisms. The septins form an hourglass-shaped collar at the mother-bud neck, which splits into two rings flanking the division plane at cytokinesis. A recent study(1) demonstrates that these two septin rings constitute diffusion barriers that create a cytokinetic compartment to retain cortical cytokinetic factors in proximity to the cleavage plane.

Copyright 2004 Wiley Periodicals, Inc.

PMID:
15612039
[PubMed - indexed for MEDLINE]
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