Abstract
The patterning of actin cytoskeleton structures in vivo is a product of spatially and temporally regulated polymer assembly balanced by polymer disassembly. While in recent years our understanding of actin assembly mechanisms has grown immensely, our knowledge of actin disassembly machinery and mechanisms has remained comparatively sparse. Saccharomyces cerevisiae is an ideal system to tackle this problem, both because of its amenabilities to genetic manipulation and live‐cell imaging and because only a single gene encodes each of the core disassembly factors: cofilin (COF1), Srv2/CAP (SRV2), Aip1 (AIP1), GMF (GMF1/AIM7), coronin (CRN1), and twinfilin (TWF1). Among these six factors, only the functions of cofilin are essential and have been well defined. Here, we investigated the functions of the nonessential actin disassembly factors by performing genetic and live‐cell imaging analyses on a combinatorial set of isogenic single, double, triple, and quadruple mutants in S. cerevisiae. Our results show that each disassembly factor makes an important contribution to cell viability, actin organization, and endocytosis. Further, our data reveal new relationships among these factors, providing insights into how they work together to orchestrate actin turnover. Finally, we observe specific combinations of mutations that are lethal, e.g., srv2Δ aip1Δ and srv2Δ crn1Δ twf1Δ, demonstrating that while cofilin is essential, it is not sufficient in vivo, and that combinations of the other disassembly factors perform vital functions. © 2015 The Authors. Cytoskeleton Published by Wiley Periodicals, Inc.
Highlights
Cells have a finite pool of actin subunits from which they assemble a variety of filamentous arrays to perform different biological tasks
A set of six ubiquitous proteins (ADF/cofilin, Srv2/ CAP, Aip1, GMF, coronin, and twinfilin) has emerged as a core set of actin disassembly machinery found in organisms as diverse as yeast and mammals (Ono, 2007; Poukkula et al, 2011; Brieher, 2013; Ono, 2013)
How such rapid actin filament turnover dynamics are achieved is only beginning to be understood, but appears to involve the filament severing protein cofilin working in concert with a core set of actin disassembly cofactors that includes Srv2/CAP, Aip1, coronin, GMF, and twinfilin
Summary
Cells have a finite pool of actin subunits from which they assemble a variety of filamentous arrays to perform different biological tasks. A set of six ubiquitous proteins (ADF/cofilin, Srv2/ CAP, Aip, GMF, coronin, and twinfilin) has emerged as a core set of actin disassembly machinery found in organisms as diverse as yeast and mammals (Ono, 2007; Poukkula et al, 2011; Brieher, 2013; Ono, 2013) Among these six factors, only the functions and mechanisms of ADF/cofilin (referred to as cofilin hereafter) are well defined, and the roles of the other proteins and how they work in concert to disassemble actin networks are still not well understood
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