Document Type

Article

Publication Date

7-5-2012

Publication Title

Molecular Biology of the Cell

Department

Department of Biological Sciences

Abstract

Septins are conserved GTP-binding proteins that assemble into heteromeric complexes that form filaments and higher-order structures in cells. What directs filament assembly, determines the size of higher-order septin structures, and governs septin dynamics is still not well understood. We previously identified two kinases essential for septin ring assembly in the filamentous fungus Ashbya gossypii and demonstrate here that the septin Shs1p is multiphosphorylated at the C-terminus of the protein near the predicted coiled-coil domain. Expression of the nonphosphorylatable allele shs1-9A does not mimic the loss of the kinase nor does complete truncation of the Shs1p C-terminus. Surprisingly, however, loss of the C-terminus or the predicted coiled-coil domain of Shs1p generates expanded zones of septin assemblies and ectopic septin fibers, as well as aberrant cell morphology. The expanded structures form coincident with ring assembly and are heteromeric. Interestingly, while septin recruitment to convex membranes is increased, septin localization is diminished at concave membranes in these mutants. Additionally, the loss of the coiled-coil leads to increased mobility of Shs1p. These data indicate the coiled-coil of Shs1p is an important negative regulator of septin ring size and mobility, and its absence may make septin assembly sensitive to local membrane curvature.

DOI

10.1091/mbc.E12-03-0207

Original Citation

Meseroll RA, Howard L, Gladfelter AS. Septin ring size scaling and dynamics require the coiled-coil region of Shs1p. Mol Biol Cell. 2012 Sep;23(17):3391-406. doi: 10.1091/mbc.E12-03-0207. Epub 2012 Jul 5. PMID: 22767579; PMCID: PMC3431940.

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