Coiled coils and SAH domains in cytoskeletal molecular motors.

Michelle Peckham

Journal: Biochemical Society transactions 2012;39(5):1142-8

PMID: 21936779

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Abstract

Cytoskeletal motors include myosins, kinesins and dyneins. Myosins move along tracks of actin filaments, whereas kinesins and dyneins move along microtubules. Many of these motors are involved in trafficking cargo in cells. However, myosins are mostly monomeric, whereas kinesins are mostly dimeric, owing to the presence of a coiled coil. Some myosins (myosins 6, 7 and 10) contain an SAH (single α-helical) domain, which was originally thought to be a coiled coil. These myosins are now known to be monomers, not dimers. The differences between SAH domains and coiled coils are described and the potential roles of SAH domains in molecular motors are discussed.

Address: Faculty of Biological Sciences, Institute for Molecular and Cellular Biology, University of Leeds, Leeds LS 9JT, UK. [email protected]

DOI: 10.1042/BST0391142

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MeSH Terms: Amino Acid Sequence, Cytoskeleton, Dyneins, Humans, Kinesins, Molecular Motor Proteins, Molecular Sequence Data, Myosins, Phylogeny, Protein Isoforms, Protein Structure, Quaternary, Protein Structure, Secondary