Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The myosin passenger protein Smy1 controls actin cable structure and dynamics by acting as a formin damper.

Developmental cell - 16 Aug 2011

Chesarone-Cataldo Melissa, Guérin Christophe, Yu Jerry H, Wedlich-Soldner Roland, Blanchoin Laurent, Goode Bruce L

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Actins
Share to Cytoskeletal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dose-Response Relationship, Drug

Share to Green Fluorescent Proteins

Share to Microfilament Proteins

Share to Myosin Type V

Share to Protein Transport

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 21839918
DOI: 10.1016/j.devcel.2011.07.004
PMCID: PMC3157649

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The myosin passenger protein Smy1 controls actin cable structure and dynamics by acting as a formin damper.PMID 21839918Read ↗

Common formin-regulating sequences in Smy1 and Bud14 are required for the control of actin cable assembly in vivo.Semantic proximity Read ↗

The F-BAR protein Hof1 tunes formin activity to sculpt actin cables during polarized growth.Semantic proximity Read ↗

Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast.Semantic proximity Read ↗

Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast.Semantic proximity Read ↗

Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function.Semantic proximity Read ↗

Genetically inspired in vitro reconstitution of Saccharomyces cerevisiae actin cables from seven purified proteins.Semantic proximity Read ↗

Stable and dynamic axes of polarity use distinct formin isoforms in budding yeast.Semantic proximity Read ↗

Myosin-V is activated by binding secretory cargo and released in coordination with Rab/exocyst function.Semantic proximity Read ↗

Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables.Semantic proximity Read ↗

A myosin passenger protein gene (FaSmy1) is an essential regulator of cell development, pathogenicity, DON biosynthesis, and resistance to the fungicide phenamacril in Fusarium asiaticumSemantic proximity Read ↗

The functionally distinct fission yeast formins have specific actin-assembly properties.Semantic proximity Read ↗

Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.