Calcium-dependent inhibition of in vitro thin-filament motility by native titin
Calcium-dependent inhibition of in vitro thin-filament motility by native titin
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DOI：
10.1016/0014-5793(96)00055-5
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发表时间：
1996-02-19
期刊：
影响因子：
3.5
通讯作者：
Granzier, HL
中科院分区：
文献类型：
--
作者：
Kellermayer, MSZ;Granzier, HL
肌联蛋白（也称为连接蛋白）是一种巨大的丝状蛋白，跨越脊椎动物肌肉肌节的Z线和NI线之间的距离，在被动张力的产生中起着重要作用。肌联蛋白已被证明与肌球蛋白强烈结合，使其与肌节中的粗丝紧密结合。最近的观察表明，肌联蛋白也与肌动蛋白相互作用的可能性，这意味着肌联蛋白在肌肉收缩中的进一步功能，我们显示-使用体外运动和结合试验-天然肌联蛋白与丝状肌动蛋白和重构细丝相互作用。这种相互作用抑制了纤维的体外运动。此外，细细丝相互作用发生在钙依赖性的方式：增加钙的结果，在增强结合的细丝肌联蛋白和更大的抑制体外运动。
Titin (also known as connectin) is a giant filamentous protein that spans the distance between the Z- and NI-lines of the vertebrate muscle sarcomere and plays a fundamental role in the generation of passive tension. Titin has been shown to bind strongly to myosin, making it tightly associated to the thick filament in the sarcomere. Recent observations have suggested the possibility that titin also interacts with actin, implying further functions of titin in muscle contraction, We show - using in vitro motility and binding assays - that native titin interacts with both filamentous actin and reconstituted thin filaments. The interaction results in the inhibition of the filaments' in vitro motility. Furthermore, the thin-thin filament interaction occurs in a calcium-dependent manner: increased calcium results in enhanced binding of thin filaments to titin and greater suppression of in vitro motility.