Cell
An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin
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Epithelial-specific isoforms of protein 4.1R promote adherens junction assembly in maturing epithelia
2020, Journal of Biological ChemistryStructure and function of Palladin's actin binding domain
2013, Journal of Molecular BiologyPlasma membrane calcium ATPase activity is regulated by actin oligomers through direct interaction
2013, Journal of Biological ChemistryCitation Excerpt :Oligomers also do not bind this domain because CaM and actin had additive effects on PMCA catalytic activity (Fig. 8). A possible candidate for the binding site may be the positively charged acidic phospholipid site in the PMCA, because actin is negatively charged at physiological pH. Lysine-rich clusters in actin-binding proteins have been identified to be involved in actin binding, e.g. the DAIKKK sequence in actin depolymerization factor, cofilin, and tropomyosin (89); the KKGGKKKG sequence of myosin (90); the KSKLKKT sequence in thymosin β4 (91), and the sequence KKEK in villin (92). Although there is no conserved sequence for actin binding between the different actin-binding proteins, a consistent motif rich in basic residues exists, which is also present in the PMCA sequence at the cytosolic loop between the transmembrane segments 2 and 3.
A gain-of-function mutation in the M-domain of cardiac myosin-binding protein-C increases binding to actin
2013, Journal of Biological Chemistry