The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle.
The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle.
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DOI：
10.3390/proteomes9010009
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发表时间：
2021-02-02
期刊：
影响因子：
3.3
通讯作者：
Ohlendieck K
中科院分区：
文献类型：
--
作者：
Dowling P;Gargan S;Murphy S;Zweyer M;Sabir H;Swandulla D;Ohlendieck K
对儿童杜氏肌营养不良症中有缺陷的DMD基因蛋白产物进行系统的生物分析表征，发现了膜细胞骨架蛋白肌营养不良蛋白。它的全长肌肉同种型Dp 427-M与肌膜相关复合物紧密连接，该复合物由肌营养不良蛋白聚糖、肌聚糖、肌节蛋白、肌营养不良蛋白和突触营养蛋白组成。除了肌养蛋白-糖蛋白复合物的这些核心成员之外，更广泛的肌养蛋白相关网络包括属于细胞内细胞骨架和微管组装、基底层和细胞外基质、各种质膜蛋白和胞质组分的关键蛋白。在这里，我们回顾了肌营养不良蛋白复合物的核心作用，作为一个主节点在肌纤维，整合细胞骨架组织和细胞信号在肌肉周边，以及提供肌膜稳定和收缩力传递到细胞外区域。优化的组织提取，亚细胞分级分离，先进的蛋白质共纯化策略，免疫沉淀，液相色谱和二维凝胶电泳与现代质谱为基础的蛋白质组学相结合，证实了核心肌营养不良蛋白复合物在肌膜膜的组成。重要的是，这些生物化学和质谱调查已经确定了更广泛的肌营养不良蛋白网络的其他成员，包括双糖蛋白聚糖，cavin，synemin，桥粒芯糖蛋白，微管蛋白，斑珠蛋白，细胞角蛋白和各种信号蛋白和离子通道。
The systematic bioanalytical characterization of the protein product of the DMD gene, which is defective in the pediatric disorder Duchenne muscular dystrophy, led to the discovery of the membrane cytoskeletal protein dystrophin. Its full-length muscle isoform Dp427-M is tightly linked to a sarcolemma-associated complex consisting of dystroglycans, sarcoglyans, sarcospan, dystrobrevins and syntrophins. Besides these core members of the dystrophin–glycoprotein complex, the wider dystrophin-associated network includes key proteins belonging to the intracellular cytoskeleton and microtubular assembly, the basal lamina and extracellular matrix, various plasma membrane proteins and cytosolic components. Here, we review the central role of the dystrophin complex as a master node in muscle fibers that integrates cytoskeletal organization and cellular signaling at the muscle periphery, as well as providing sarcolemmal stabilization and contractile force transmission to the extracellular region. The combination of optimized tissue extraction, subcellular fractionation, advanced protein co-purification strategies, immunoprecipitation, liquid chromatography and two-dimensional gel electrophoresis with modern mass spectrometry-based proteomics has confirmed the composition of the core dystrophin complex at the sarcolemma membrane. Importantly, these biochemical and mass spectrometric surveys have identified additional members of the wider dystrophin network including biglycan, cavin, synemin, desmoglein, tubulin, plakoglobin, cytokeratin and a variety of signaling proteins and ion channels.
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DOI：
10.1016/j.bbrc.2006.05.192
发表时间：
2006-08-04
影响因子：
3.1
作者：
Bhosle, Rahul C.;Michele, Daniel E.;Robson, Richard M.
通讯作者：
Robson, Richard M.
影响因子：
64.5
作者：
BONILLA, E;SAMITT, CE;ROWLAND, LP
通讯作者：
ROWLAND, LP
影响因子：
--
作者：
Abramovici, Hanan;Gee, Stephen H.
通讯作者：
Gee, Stephen H.
影响因子：
2.5
作者：
Belhasan DC;Akaaboune M
通讯作者：
Akaaboune M
影响因子：
6.4
作者：
Blake, DJ;Tinsley, JM;Davies, KE
通讯作者：
Davies, KE