Supporting information

Myosins are a large family of motor proteins that share the common features of ATP hydrolysis (ATPase enzyme activity), actin binding and potential for kinetic energy transduction. Originally isolated from muscle cells (hence the name), almost all eukaryotic cells are now known to contain myosins.

Structurally, mysoins contain a 'head' domain that binds to actin filaments (microfilaments) and is the site of ATP hydrolysis. The 'tail' domain interacts with cargo molecules, and the 'neck' acts as a linker between the head and tail and is the site of regulatory myosin light chain binding.

There are 17 myosin families and the most well characterized is myosin II. Myosin II is found predominantly in myocytes and mediates plus-ended movement along microfilaments. It is involved in muscle contraction through cyclic interactions with actin-rich thin filaments, creating a contractile force. It is regulated by phosphorylation via Myosin Light Chain Kinase (MLCK) and by intracellular Ca2+ concentrations.

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
Myosin IA Human MYO1A NM_005379 Q9UBC5
Mouse Myo1a NM_001081219 O88329
Rat Myo1a XM_238479 Q62774
Myosin IB Human MYO1B NM_012223 O43795
Mouse Myo1b NM_010863 P46735
Rat Myo1b NM_053986 Q05096
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Literature for Myosin

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