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Reining in cytokinesis with a septin corral
Author(s) -
Finger Fern P.
Publication year - 2005
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.20167
Subject(s) - septin , cytokinesis , microbiology and biotechnology , cell division , cleavage furrow , biology , cleavage (geology) , budding yeast , yeast , saccharomyces cerevisiae , genetics , cell , paleontology , fracture (geology)
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 study1 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. BioEssays 27:5–8, 2005. © 2004 Wiley Periodicals, Inc.