The cysteine-rich and C-terminal domains of dystrophin are not required for normal costameric localization in the mouse
The cysteine-rich and C-terminal domains of dystrophin are not required for normal costameric localization in the mouse
复制标题
抗肌营养不良蛋白的富含半胱氨酸和 C 末端结构域对于小鼠的正常肋节定位来说不是必需的
DOI：
10.1007/bf01969430
复制
发表时间：
1996
影响因子：
3
通讯作者：
S. Brown
中科院分区：
文献类型：
--
作者：
M. Maconochie;A. H. Simpkins;E. Damien;G. Coulton;A. Greenfield;S. Brown
肌营养不良蛋白具有模块化结构，并且被认为通过将细胞骨架连接到细胞外基质而对肌细胞细胞结构至关重要。N-末端与肌动蛋白结合，C-末端的两个结构域，富含半胱氨酸的结构域和C-末端结构域，通过肌营养不良蛋白聚糖复合物间接与肌膜结合。我们已经在小鼠胚胎干（ES）细胞中产生了突变，该突变用于删除富含半胱氨酸的结构域和C-末端结构域，以直接解决它们的作用。我们表明，这两个领域是没有必要的正常costameric组织在肌膜来自突变细胞系的肌管。此外，在小鼠体内嵌合体肌肉中，肌膜定位也是明显的。
Dystrophin has a modular structure and is believed to be critical for muscle cell cytoarchitecture by linking the cytoskeleton to the extracellular matrix. The N-terminus binds to actin and two domains at the C-terminus, the cysteine-rich and C-terminal domains, are associated with the sarcolemma indirectly via the dystroglycan complex. We have generated a mutation in mouse embryonic stem (ES) cells which serves to delete the cysteine-rich and C-terminal domains to address directly their role. We show that these two domains are not necessary for normal costameric organization at the sarcolemma in myotubes derived from the mutant cell line. Furthermore sarcolemmal localization is also apparent in mouse chimaeric musclein vivo.