InterPro domain: IPR010926

Class I myosins (Myo1s) are widely expressed in eukaryotic cells. Myo1s existas monomers and can sense cellular mechanical forces and function as tension-sensitive anchors or transporters. Each Myo1 contains from N terminus to Cterminus, a motor domain, a neck region consisting ofseveral calmodulin (CaM)-binding IQ motifs and a tailregion. All Myo1s contain a tail homology (TH1) domain featuring an embeddedpleckstrin-homology (PH) domain capable of binding to lipidmembranes. In addition, Myo1s with long tails also contain a TH2 (or GPA)domain and a C-terminal TH3 (or SH3) domain, the latter ofwhich may be responsible for binding to cargos. All Myo1s are capable ofbridging actin cytoskeletons with lipid membranes by using their motor headsand tail TH1 domains.

The TH1 domain is an extended PH domain capable ofbinding to lipids [ 1 , 2 ].

1. Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling. Nat. Struct. Mol. Biol. 22, 81-8
2. Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH). J. Biol. Chem. 285, 8675-86