S100a0蛋白与肌动蛋白封端蛋白CapZ的相互作用：CapZα亚基中一个假定的S100a0结合位点的特性分析

Interaction of S100a0 protein with the actin capping protein, CapZ: characterization of a putative S100a0 binding site in CapZ alpha-subunit.

作者信息

Ivanenkov V V, Dimlich R V, Jamieson G A

机构信息

Department of Emergency Medicine, University of Cincinnati College of Medicine, Ohio 45267, USA.

出版信息

Biochem Biophys Res Commun. 1996 Apr 5;221(1):46-50. doi: 10.1006/bbrc.1996.0542.

DOI:10.1006/bbrc.1996.0542

PMID:8660341

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.

摘要

S100a0是一种主要在心肌和骨骼肌组织中表达的钙结合蛋白，通过化学交联证明它能以钙依赖的方式与肌动蛋白封端蛋白CapZ相互作用。TRTK-12是CapZalpha羧基末端区域内包含的一种肽，它以剂量依赖的方式抑制S100a0与CapZ的相互作用。通过交联显示TRTK-12在有钙存在的情况下能结合S100a0，通过荧光分光光度法显示它能以可饱和的方式与阴离子磷脂以及CapZ活性调节剂磷脂酰肌醇4-单磷酸相互作用；但不与中性磷脂磷脂酰胆碱相互作用。这些数据表明S100a0和多磷酸肌醇结合到CapZalpha的同一个羧基末端区域，从而可能调节CapZ的活性。