The F-actin binding domain forms a compact bundle of four antiparallel α-helices, which are arranged in a left-handed topology. Binding of F-actin to the F-actin binding domain may result in cytoplasmic retention and subcellular distribution of the protein, as well as possible inhibition of protein function [ PUBMED:16109371 … expand

The F-actin binding domain forms a compact bundle of four antiparallel α-helices, which are arranged in a left-handed topology. Binding of F-actin to the F-actin binding domain may result in cytoplasmic retention and subcellular distribution of the protein, as well as possible inhibition of protein function [ PUBMED:16109371 ]. Proteins containing this domain include tyrosine-protein kinases Abl1, which is a non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis [ PUBMED:9037071 PUBMED:11971963 ]. Abl1 is linked to different forms of leukemia in humans.