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Interaction of S100a0 protein with the actin capping protein, CapZ: characterization of a putative S100a0 binding
V V Ivanenkov1, R V Dimlich, G A Jamieson
1Department of Emergency Medicine, University of Cincinnati College of Medicine, Ohio 45267, USA.
Abstract:
S100a0, a Ca2+-binding protein expressed predominantly in cardiac and skeletal muscle tissues, was demonstrated by chemical cross-linking to interact in a Ca2+ -dependent manner with the actin capping protein CapZ. TRTK-12, a peptide contained within the COOH-terminal region of CapZalpha, inhibited S100a0: CapZ interaction in a dose-dependent manner. TRTK-12 was shown by cross-linking to bind S100a0 in the presence of Ca2+, and by fluorescence spectrophotometry to interact in a saturable manner with the anionic phospholipid and a regulator of CapZ activity, phosphatidylinositol 4-monophosphate; but not with the neutral phospholipid, phosphatidylcholine. These data suggest S100a0 and polyphosphoinositides bind to the same COOH-terminal region of CapZalpha, thus potentially modulating CapZ activity.