The role of Bni5 in the regulation of septin higher-order structure formation

Biological Chemistry
Csilla PatasiMarian Farkašovský

Abstract

Septins are a family of conserved cytoskeletal proteins playing an essential role in cytokinesis and in many other cellular processes in fungi and animals. In budding yeast Saccharomyces cerevisiae, septins form filaments and higher-order structures at the mother-bud neck depending on the particular stage of the cell cycle. Septin structures at the division plane serve as a scaffold to recruit the proteins required for particular cellular processes. The formation and localization of septin structures at particular stages of the cell cycle also determine functionality of these proteins. Many different proteins participate in regulating septin assembly. Despite recent developments, we are only beginning to understand how specific protein-protein interactions lead to changes in the polymerization of septin filaments or assembly of higher-order structures. Here, using fluorescence and electron microscopy, we found that Bni5 crosslinks septin filaments into networks by bridging pairs or multiple filaments, forming structures that resemble railways. Furthermore, Bni5 appears to be a substrate of the Elm1 protein kinase in vitro. Moreover, Elm1 induces in the presence of Bni5 disassembly of long septin filaments, suggesting that these...Continue Reading

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Citations

Feb 5, 2016·Seminars in Cell & Developmental Biology·Franz Meitinger, Saravanan Palani
Apr 18, 2016·Cellular and Molecular Life Sciences : CMLS·Maria Angeles Juanes, Simonetta Piatti
Jan 9, 2020·Biological Chemistry·Marian Farkašovský
Nov 17, 2016·Frontiers in Cell and Developmental Biology·Adam M PerezJeremy Thorner
Jul 7, 2018·Cytoskeleton·Joseph MarquardtErfei Bi
May 7, 2021·Frontiers in Cellular and Infection Microbiology·Alexander A Morano, Jeffrey D Dvorin

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Methods Mentioned

BETA
fluorescence microscopy
two-hybrid
electrophoresis
PCR
fluorescence
electron microscopy
GTPase

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