Functional redundancy and formin-independent localization of tropomyosin isoforms in Saccharomyces cerevisiae.

ABSTRACT: Tropomyosin is an actin binding protein which protects actin filaments from cofilin-mediated disassembly. Distinct tropomyosin isoforms have long been hypothesized to differentially sort to subcellular actin networks and impart distinct functionalities. Nevertheless, a mechanistic understanding of the interplay between Tpm isoforms and their functional contributions to actin dynamics has been lacking. In this study, we present and charcaterize mNeonGreen-Tpm fusion proteins that exhibit good functionality in cells as a sole copy, surpassing limitations of existing probes and enabling real-time dynamic tracking of Tpm-actin filaments in vivo. Using these functional Tpm fusion proteins, we find that S. cerevisiae Tpm isoforms, Tpm1 and Tpm2, colocalize on actin cables and indis

SUBMITTER: Dhar A 

PROVIDER: S-EPMC11014519 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature