Sequential recruitment of F-BAR proteins controls cytoskeletal crosstalk at the yeast bud neck.

ABSTRACT: In vivo functions of the septin and actin cytoskeletons are closely intertwined, yet the mechanisms underlying septin-actin crosstalk have remained poorly understood. Here, we show that the yeast-bud-neck-associated Fes/CIP4 homology Bar-amphiphysin-Rvs (F-BAR) protein suppressor of yeast profilin 1 (Syp1)/FCHo uses its intrinsically disordered region (IDR) to directly bind and bundle filamentous actin (F-actin) and to physically link septins and F-actin. Interestingly, the only other F-BAR protein found at the neck during bud development, Hof1, has related activities and also potently inhibits the bud-neck-associated formin Bnr1. However, we find that Syp1 enhances rather than inhibits Bnr1-mediated actin assembly and fully overcomes Hof1-mediated inhibition of Bnr1. Further, during bud d

SUBMITTER: Magliozzi JO 

PROVIDER: S-EPMC11794016 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature