Motor Function of Unconventional Myosin View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2003

AUTHORS

Mitsuo Ikebe , Akira Inoue , So Nishikawa , Kazuaki Homma , Hiroto Tanaka , Atsuko Hikikoshi Iwane , Eisaku Katayama , Reiko Ikebe , Toshio Yanagida

ABSTRACT

Myosins are motor proteins that interact with actin filaments and convert energy from ATP hydrolysis into mechanical force. In addition to the well-characterized conventional, filament forming, two-headed myosin II of muscle and non-muscle cells, a number of myosin-like proteins have recently been discovered. Based upon their amino acid sequences, these newly found “myosins” do not seem to form myosin filaments, thus they are often called “unconventional” myosins. The discovery of these “myosin-like motor proteins” has fundamentally expanded the potential physiological importance of myosins in diverse biological processes such as chemotactic motility, endocytosis, exocytosis, phagocytosis, vesicular trafficking, secretion, etc. The myosins are classified based upon phylogenetie sequence comparisons of the motor domain (Cheney et al, 1993; Goodson and Spudich, 1993; Mooseker and Cheney, 1995; Cope et al, 1996; Titus, 1997; Hodge and Cope, 2000) and divided into at least 18 classes. In vertebrates, it has been shown that eleven classes of myosin, (including conventional filament forming myosin) are expressed. The N-terminal domains of these classes of unconventional myosins are relatively conserved and contain the primary force production machinery, whereas the C-terminal tail domains are highly divergent and are thought to function as targeting sites that bind to the cellular partner molecules. Between the motor and the diverse tail domains of myosin, there are neck regions that are composed of various numbers of light chain binding motifs (Mermall et al, 1998). More... »

PAGES

143-157

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4419-9029-7_13

DOI

http://dx.doi.org/10.1007/978-1-4419-9029-7_13

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038179703

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15098662


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