The Myosin passenger protein smy1 controls actin cable structure and dynamics by acting as a formin damper.

19:02 EST 28th November 2014 | BioPortfolio

Summary of "The Myosin passenger protein smy1 controls actin cable structure and dynamics by acting as a formin damper."

Formins are a conserved family of proteins with robust effects in promoting actin nucleation and elongation. However, the mechanisms restraining formin activities in cells to generate actin networks with particular dynamics and architectures are not well understood. In S. cerevisiae, formins assemble actin cables, which serve as tracks for myosin-dependent intracellular transport. Here, we show that the kinesin-like myosin passenger-protein Smy1 interacts with the FH2 domain of the formin Bnr1 to decrease rates of actin filament elongation, which is distinct from the formin displacement activity of Bud14. In vivo analysis of smy1Δ mutants demonstrates that this "damper" mechanism is critical for maintaining proper actin cable architecture, dynamics, and function. We directly observe Smy1-3GFP being transported by myosin V and transiently pausing at the neck in a manner dependent on Bnr1. These observations suggest that Smy1 is part of a negative feedback mechanism that detects cable length and prevents overgrowth.

Affiliation

Department of Biology and Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, MA 02454, USA.

Journal Details

This article was published in the following journal.

Name: Developmental cell
ISSN: 1878-1551
Pages: 217-30

Links

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Medical and Biotech [MESH] Definitions

One of the minor protein components of skeletal muscle. Its function is to serve as the calcium-binding component in the troponin-tropomyosin B-actin-myosin complex by conferring calcium sensitivity to the cross-linked actin and myosin filaments.

A PROFILIN binding domain protein that is part of the Arp2-3 complex. It is related in sequence and structure to ACTIN and binds ATP.

A subclass of myosins found generally associated with actin-rich membrane structures such as filopodia. Members of the myosin type I family are ubiquitously expressed in eukaryotes. The heavy chains of myosin type I lack coiled-coil forming sequences in their tails and therefore do not dimerize.

An actin capping protein that binds to the barbed-ends of ACTIN filaments. It is a heterodimer consisting of an alpha and a beta subunit. It regulates actin assembly by stabilizing actin oligomers for elongation. In SKELETAL MUSCLE, CapZ is localized to the Z-disk.

A component of the Arp2-3 complex that is related in sequence and structure to ACTIN and that binds ATP. It is expressed at higher levels than ARP2 PROTEIN and does not contain a PROFILIN binding domain.

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