Structural highlights
Function
[CDC11_YEAST] Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.[1]
Publication Abstract from PubMed
Septins are a conserved family of GTP-binding proteins that assemble into a highly ordered array of filaments at the mother bud neck in Saccharomyces cerevisiae cells. Many molecular functions and mechanisms of the septins in S. cerevisiae were already uncovered. However, structural information is only available from modeling the crystallized subunits of the human septins into the EM cryomicroscopy data of the yeast hetero-octameric septin rod. Octameric rods are the building block of septin filaments in yeast. We present here the first crystal structure of Cdc11, the terminal subunit of the octameric rod and discuss its structure in relation to its human homologues. Size exclusion chromatography analysis revealed that Cdc11 forms homodimers through its C-terminal coiled coil tail.
Crystal structure of Cdc11, a septin subunit from Saccharomyces cerevisiae.,Brausemann A, Gerhardt S, Schott AK, Einsle O, Grosse-Berkenbusch A, Johnsson N, Gronemeyer T J Struct Biol. 2016 Jan 9. pii: S1047-8477(16)30003-X. doi:, 10.1016/j.jsb.2016.01.004. PMID:26780475[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Casamayor A, Snyder M. Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function. Mol Cell Biol. 2003 Apr;23(8):2762-77. PMID:12665577
- ↑ Brausemann A, Gerhardt S, Schott AK, Einsle O, Grosse-Berkenbusch A, Johnsson N, Gronemeyer T. Crystal structure of Cdc11, a septin subunit from Saccharomyces cerevisiae. J Struct Biol. 2016 Jan 9. pii: S1047-8477(16)30003-X. doi:, 10.1016/j.jsb.2016.01.004. PMID:26780475 doi:https://dx.doi.org/10.1016/j.jsb.2016.01.004
