肌节M带结构蛋白M蛋白中肌球蛋白结合结构域和调节性磷酸化位点的定位
Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band.
作者信息
Obermann W M, van der Ven P F, Steiner F, Weber K, Fürst D O
机构信息
Max-Planck-Institute for Biophysical Chemistry, Department of Biochemistry, D-37077 Göttingen, Germany.
出版信息
Mol Biol Cell. 1998 Apr;9(4):829-40. doi: 10.1091/mbc.9.4.829.
Abstract
The myofibrils of cross-striated muscle fibers contain in their M bands cytoskeletal proteins whose main function seems to be the stabilization of the three-dimensional arrangement of thick filaments. We identified two immunoglobin domains (Mp2-Mp3) of M-protein as a site binding to the central region of light meromyosin. This binding is regulated in vitro by phosphorylation of a single serine residue (Ser76) in the immediately adjacent amino-terminal domain Mp1. M-protein phosphorylation by cAMP-dependent kinase A inhibits binding to myosin LMM. Transient transfection studies of cultured cells revealed that the myosin-binding site seems involved in the targeting of M-protein to its location in the myofibril. Using the same method, a second myofibril-binding site was uncovered in domains Mp9-Mp13. These results support the view that specific phosphorylation events could be also important for the control of sarcomeric M band formation and remodeling.
摘要
横纹肌纤维的肌原纤维在其M带中含有细胞骨架蛋白，其主要功能似乎是稳定粗肌丝的三维排列。我们确定了M蛋白的两个免疫球蛋白结构域（Mp2-Mp3）是与轻酶解肌球蛋白中央区域结合的位点。这种结合在体外受紧邻的氨基末端结构域Mp1中单个丝氨酸残基（Ser76）磷酸化的调节。cAMP依赖性蛋白激酶A对M蛋白的磷酸化抑制了其与肌球蛋白LMM的结合。培养细胞的瞬时转染研究表明，肌球蛋白结合位点似乎参与了M蛋白在肌原纤维中定位的靶向过程。使用相同方法，在结构域Mp9-Mp13中发现了第二个肌原纤维结合位点。这些结果支持以下观点，即特定的磷酸化事件对于肌节M带形成和重塑的控制也可能很重要。
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本文引用的文献
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Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin.肌节M带的分子结构：肌间蛋白中肌联蛋白和肌球蛋白结合结构域的定位以及肌间蛋白中一个潜在调节性磷酸化位点的鉴定。
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The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy.肌节M带的结构：通过免疫电子显微镜确定肌间蛋白、M蛋白和肌联蛋白250-kD羧基末端区域的结构域定位。
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The globular head domain of titin extends into the center of the sarcomeric M band. cDNA cloning, epitope mapping and immunoelectron microscopy of two titin-associated proteins.肌联蛋白的球状头部结构域延伸至肌节M带的中心。两种肌联蛋白相关蛋白的cDNA克隆、表位作图及免疫电子显微镜研究。
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A new 185,000-dalton skeletal muscle protein detected by monoclonal antibodies.一种由单克隆抗体检测到的185,000道尔顿的新型骨骼肌蛋白。
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