Myosin light chain kinase colocalizes with nonmuscle myosin IIB in myofibril precursors and sarcomeric Z-lines of cardiomyocytes

Myosin light chain kinase colocalizes with nonmuscle myosin IIB in myofibril precursors and sarcomeric Z-lines of cardiomyocytes
复制标题

DOI:
10.1002/cm.20127
复制
发表时间:
2006-07-01
影响因子:
--
通讯作者:
Shirinsky, V. R.
Shirinsky, V. R.
中科院分区:
其他
文献类型:
--
作者:
Dudnakova, T. V.;Stepanova, O. V.;Shirinsky, V. R.

文献摘要

被引文献

相似文献

肌球蛋白轻链激酶(MLCK)是涉及肌动蛋白和肌球蛋白II的各种形式的细胞运动的关键调节因子。MLCK广泛存在于包括心肌在内的脊椎动物组织中。然而,MLCK在心肌细胞功能中的作用尚不清楚。以前试图深入了解可能的作用和确定潜在的分子伴侣是令人失望的和模棱两可的,由于交叉反应的早期抗体与横纹肌MLCK,它具有不同的遗传基因座和不同的氨基酸序列从上述酶。使用免疫荧光方法和一组针对MLCK、细胞骨架和肌节蛋白的抗体,我们将MLCK定位于胚胎和成人心肌细胞的肌原纤维前体和肌节Z线。相同的结构含有非肌肉肌球蛋白IIB,暗示这种蛋白质可能是MLCK的靶点。我们的研究结果表明,MLCK在心肌细胞的分化和收缩,通过调节非肌肉肌球蛋白IIB的作用。
Myosin light chain kinase (MLCK) is a key regulator of various forms of cell motility involving actin and myosin II. MLCK is widely present in vertebrate tissues including the myocardium. However, the role of MLCK in cardiomyocyte function is not known. Previous attempts to gain insight into possible roles and identify potential molecular partners were disappointing and equivocal due to cross reactivity of early antibodies with striated muscle MLCK, which has a different genetic locus and a divergent amino acid sequence from the abovementioned enzyme. Using an immunofluorescence approach and a panel of antibodies directed against MLCK, cytoskeletal, and sarcomeric proteins, we localized MLCK to myofibril precursors and Z-lines of sarcomeres in embryonic and adult cardiomyocytes. The same structures contained nonmuscle myosin IIB implicating this protein as a possible target of MLCK. Our results suggest a role for MLCK in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin IIB.