The role of tropomyosin in the interactions of F-actin with caldesmon and actin-binding protein (or filamin).
The role of tropomyosin in the interactions of F-actin with caldesmon and actin-binding protein (or filamin).
复制标题
原肌球蛋白在 F-肌动蛋白与钙结合蛋白和肌动蛋白结合蛋白（或细丝蛋白）相互作用中的作用。
DOI：
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Koscak Maruyama
中科院分区：
文献类型：
--
作者：
Masao Nomura;Kunihiko Yoshikawa;Toshihiko Tanaka;Kenji Sobue;Koscak Maruyama
用落球粘度法、结合试验和电镜技术研究了肌动蛋白丝与肌动蛋白结合蛋白（细丝蛋白）和钙调素的相互作用。Caldesmon降低细丝蛋白与F-肌动蛋白的结合常数。相反，细丝蛋白与F-肌动蛋白的最大结合能力被原肌球蛋白降低。微丝蛋白诱导的肌动蛋白丝凝胶化被钙调素抑制。原肌球蛋白也抑制这种凝胶化。在原肌球蛋白的影响下，钙调素的作用增强。此外，钙调蛋白和原肌球蛋白还降低了细丝蛋白与F-肌动蛋白的结合。从这些结果来看，钙调蛋白和原肌球蛋白似乎影响细丝蛋白与不同模式的肌动蛋白的F-肌动蛋白结合。此外，从凝胶过滤判断，细丝蛋白、钙调蛋白和原肌球蛋白之间没有直接相互作用的迹象。在钙调素和原肌球蛋白的影响下，钙调素赋予微丝蛋白诱导的肌动蛋白丝凝胶化的Ca 2+敏感性。
The interactions of actin filaments with actin-binding protein (filamin) and caldesmon under the influence of tropomyosin were studied in detail using falling-ball viscometry, binding assay and electron microscopy. Caldesmon decreased the binding constant of filamin with F-actin. In contrast, the maximum binding ability of filamin to F-actin was decreased by tropomyosin. The filamin-induced gelation of actin filaments was inhibited by caldesmon. Tropomyosin also inhibited this gelation. The effect of caldesmon became stronger under the influence of tropomyosin. Furthermore, both caldesmon and tropomyosin additionally decreased the filamin binding to F-actin. From these results, caldesmon and tropomyosin appeared to influence filamin binding to F-actin with different modes of actin. In addition, there was no sign of direct interactions between filamin, caldesmon and tropomyosin as judged from gel filtration. Under the influence of caldesmon and tropomyosin, calmodulin conferred Ca2+ sensitivity on the filamin-induced gelation of actin filaments.
影响因子：
5.6
作者：
HARTWIG, JH;STOSSEL, TP
通讯作者：
STOSSEL, TP