Format

Send to

Choose Destination
See comment in PubMed Commons below
Trends Cell Biol. 2010 Jul;20(7):418-26. doi: 10.1016/j.tcb.2010.04.004. Epub 2010 May 12.

Leveraging the membrane - cytoskeleton interface with myosin-1.

Author information

1
Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37205, USA.

Abstract

Class 1 myosins are small motor proteins with the ability to simultaneously bind to actin filaments and cellular membranes. Given their ability to generate mechanical force, and their high prevalence in many cell types, these molecules are well positioned to carry out several important biological functions at the interface of membrane and the actin cytoskeleton. Indeed, recent studies implicate these motors in endocytosis, exocytosis, release of extracellular vesicles, and the regulation of tension between membrane and the cytoskeleton. Many class 1 myosins also exhibit a load-dependent mechano-chemical cycle that enables them to maintain tension for long periods of time without hydrolyzing ATP. These properties put myosins-1 in a unique position to regulate dynamic membrane-cytoskeleton interactions and respond to physical forces during these events.

PMID:
20471271
PMCID:
PMC2897960
DOI:
10.1016/j.tcb.2010.04.004
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center