[HTML][HTML] Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain

JN Mazerik, MJ Tyska - Journal of Biological Chemistry, 2012 - ASBMB
One of the most abundant components of the enterocyte brush border is the actin-based
monomeric motor, myosin-1a (Myo1a). Within brush border microvilli, Myo1a carries out a
number of critical functions at the interface between membrane and actin cytoskeleton.
Proper physiological function of Myo1a depends on its ability to bind to microvillar
membrane, an interaction mediated by a C-terminal tail homology 1 (TH1) domain.
However, little is known about the mechanistic details of the Myo1a-TH1/membrane …