Rab8-optineurin-myosin VI: analysis of interactions and functions in the secretory pathway.
Rab8-optineurin-myosin VI: analysis of interactions and functions in the secretory pathway.
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DOI：
10.1016/s0076-6879(07)38002-6
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发表时间：
2008
影响因子：
--
通讯作者：
Buss, Folma
中科院分区：
文献类型：
--
作者：
Chibalina, Margarita V.;Roberts, Rhys C.;Arden, Susan D.;Kendrick-Jones, John;Buss, Folma
小的GTPase Rab8已被证明调节从TGN到细胞表面的极化膜运输途径。Optineurin是Rab8的效应蛋白，也是基于肌动蛋白的运动蛋白肌球蛋白VI的结合伙伴。在我们的实验室中，我们用各种方法研究了肌球蛋白VI与其结合伙伴之间的相互作用，并分析了它们在细胞膜转运途径中的作用(S)。在本章中，我们描述了使用哺乳动物双杂交试验来演示蛋白质-蛋白质相互作用并确定结合位点。我们描述了一种分泌实验，结合RNA干扰技术来分析肌球蛋白VI、视神经磷酸酶和Rab8在胞膜转运途径中的功能。
The small GTPase Rab8 has been shown to regulate polarised membrane trafficking pathways form the TGN to the cell surface. Optineurin is an effector protein of Rab8 and a binding partner of the actin based motor protein myosin VI. In our lab we used various approaches to study the interactions between myosin VI and its binding partners and to analyse their role(s) in intracellular membrane trafficking pathways. In this chapter we describe the use of the mammalian two-hybrid assay to demonstrate protein-protein interactions and to identify binding sites. We describe a secretion assay, which was used in combination with RNA interference technology to analyse the function of myosin VI, optineurin and Rab8 in exocytic membrane trafficking pathways.