A putative ariadne-like E3 ubiquitin ligase (PAUL) that interacts with the muscle-specific kinase (MuSK)
A putative ariadne-like E3 ubiquitin ligase (PAUL) that interacts with the muscle-specific kinase (MuSK)
复制标题
DOI：
10.1016/s1567-133x(03)00146-7
复制
发表时间：
2004-01-01
影响因子：
1.2
通讯作者：
Sanes, JR
中科院分区：
文献类型：
--
作者：
Bromann, PA;Weiner, JA;Sanes, JR
骨骼肌神经肌肉接头（NMJ）处突触后膜的形成需要肌肉特异性受体酪氨酸激酶（MuSK）的激活。已知很少有MuSK作用的细胞内介质或调节剂。E3泛素连接酶可能起此作用，因为几种受体酪氨酸激酶、G蛋白偶联受体和通道的活性受泛素化调节。在这里，我们报告识别一个假定的Ariadne样泛素连接酶（PAUL），结合到MuSK的胞质结构域。PAUL在发育和成年小鼠的许多组织中表达，并且存在于肌纤维中的NMJ处，但不限于它们。(C)2003 Elsevier B.V.保留所有权利。
Formation of the postsynaptic membrane at the skeletal neuromuscular junction (NMJ) requires activation of the muscle-specific receptor tyrosine kinase (MuSK). Few intracellular mediators or modulators of MuSK actions are known. E3 ubiquitin ligases may serve this role, because activities of several receptor tyrosine kinases, G-protein-coupled receptors and channels are modulated by ubiquitination. Here, we report identification of a putative Ariadne-like ubiquitin ligase (PAUL) that binds to the cytoplasmic domain of MuSK. PAUL is expressed in numerous tissues of developing and adult mice, and is present at NMJs in muscle fibers but is not confined to them. (C) 2003 Elsevier B.V. All rights reserved.