A septin-Hof1 scaffold at the yeast bud neck binds and organizes actin cables.

ABSTRACT: Cellular actin arrays are often highly organized, with characteristic patterns critical to their in vivo functions, yet the mechanisms for establishing these higher order geometries remain poorly understood. In Saccharomyces cerevisiae, formin-polymerized actin cables are spatially organized and aligned along the mother-bud axis to facilitate polarized vesicle traffic. Here, we show that the bud neck-associated F-BAR protein Hof1, independent of its functions in regulating the formin Bnr1, binds to actin filaments and organizes actin cables in vivo. Hof1 bundles actin filaments and links them to septins in vitro. F-actin binding is mediated by the "linker" domain of Hof1, and its deletion leads to cable organization defects in vivo. Using superresolution imaging, we show that Hof1 a

SUBMITTER: Garabedian MV 

PROVIDER: S-EPMC7543067 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature