Effects of Bni5 Binding on Septin Filament Organization

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Effects of Bni5 Binding on Septin Filament Organization.

Septins are a protein family found in all eukaryotes (except higher plants) that have roles in membrane remodeling and formation of diffusion barriers and as a scaffold to recruit other proteins. In budding yeast, proper execution of cytokinesis and cell division requires the formation of a collar of circumferential filaments at the bud neck. These filaments are assembled from apolar septin het...

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Septin filament organization in Saccharomyces cerevisiae

Septins are a family of GTP-binding, membrane-interacting cytoskeletal proteins, highly conserved and essential in all eukaryotes (with the exception of plants). Septins play important roles in a number of cellular events that involve membrane remodeling and compartmentalization. One such event is cytokinesis, the last stage of cell division. While cytokinesis is ultimately achieved via the mec...

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GTP Binding Induces Filament Assembly of a Recombinant Septin

The septins are a family of GTPases involved in cytokinesis in budding yeast, Drosophila, and vertebrates (see for review). Septins are associated with a system of 10 nm filaments at the S. cerevisiae bud neck, and heteromultimeric septin complexes have been isolated from cell extracts in a filamentous state. A number of septins have been shown to bind and hydrolyze guanine nucleotide. However,...

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Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae.

Mitotic yeast (Saccharomyces cerevisiae) cells express five related septins (Cdc3, Cdc10, Cdc11, Cdc12, and Shs1) that form a cortical filamentous collar at the mother-bud neck necessary for normal morphogenesis and cytokinesis. All five possess an N-terminal GTPase domain and, except for Cdc10, a C-terminal extension (CTE) containing a predicted coiled coil. Here, we show that the CTEs of Cdc3...

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Crosslinks and molecular motors play an important role in the organization of cytoskeletal filament networks. Here we incorporate the effect of crosslinks into our model of polar motor-filament organization [Phys. Rev. E 71, 050901 (2005)], through suppressing the relative sliding of filaments in the course of motor-mediated alignment. We show that this modification leads to a nontrivial macros...

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ژورنال

عنوان ژورنال: Journal of Molecular Biology

سال: 2016

ISSN: 0022-2836

DOI: 10.1016/j.jmb.2016.10.024