Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the voltage-gated potassium channel Kv1.5
Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the voltage-gated potassium channel Kv1.5
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DOI：
10.1152/ajpheart.00152.2004
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发表时间：
2004-08-01
影响因子：
4.8
通讯作者：
Koren, G
中科院分区：
文献类型：
--
作者：
Folco, EJ;Liu, GX;Koren, G
离子通道靶向特定的膜微区和它们在大分子复合物中的组织允许可兴奋细胞有效地响应细胞外信号。在这项研究中，我们描述了一个复杂的形成，包含两个支架蛋白：小窝蛋白-3（Cav-3）和膜相关鸟苷酸激酶（MAGUK），SAP 97。复合物的形成涉及Cav-3与位于其PDZ 2和PDZ 3结构域之间的SAP 97片段的缔合。在异源表达系统中，该支架复合物可以募集Kv1.5以形成三重复合物，其中三个组分中的每一个与其他两个相互作用。这些相互作用调节由Kv1.5的糖基化缺陷突变体编码的电流的表达。我们的结论是，协会的Cav-3与SAP 97可能构成的成核网站的组装含有钾通道的大分子复合物。
The targeting of ion channels to particular membrane microdomains and their organization in macromolecular complexes allow excitable cells to respond efficiently to extracellular signals. In this study, we describe the formation of a complex that contains two scaffolding proteins: caveolin-3 (Cav-3) and a membrane-associated guanylate kinase (MAGUK), SAP97. Complex formation involves the association of Cav-3 with a segment of SAP97 localized between its PDZ2 and PDZ3 domains. In heterologous expression systems, this scaffolding complex can recruit Kv1.5 to form a tripartite complex in which each of the three components interacts with the other two. These interactions regulate the expression of currents encoded by a Glycosylation-deficient mutant of Kv1.5. We conclude that the association of Cav-3 with SAP97 may constitute the nucleation site for the assembly of macromolecular complexes containing potassium channels.