CORVET and HOPS tethering complexes - coordinators of endosome and lysosome fusion
CORVET and HOPS tethering complexes - coordinators of endosome and lysosome fusion
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DOI：
10.1242/jcs.107805
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发表时间：
2013-03-15
影响因子：
4
通讯作者：
Ungermann, Christian
中科院分区：
文献类型：
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作者：
Balderhaar, Henning J. Kleine;Ungermann, Christian
蛋白质和脂质沿着真核细胞内溶酶体系统的转运取决于多重融合和裂变事件。在过去的几年里，裂变和聚变机器的分子成分都已被确定。在这里，我们重点关注内体、液泡和溶酶体的膜融合机制，特别是 CORVET 和 HOPS 两种同源束缚复合物的作用。两种复合物都是异六聚体；它们共享四个亚基，与 Rab GTP 酶和可溶性 NSF 附着蛋白受体 (SNARE) 相互作用，并且可以束缚膜。由于特定亚基的存在，CORVET 是 Rab5 效应复合物，而 HOPS 可以通过 Rab7 有效结合晚期内体和溶酶体。基于最近描述的 HOPS 复合物的整体结构和大量体内和体外分析，获得了对其功能的重要见解。在这里，我们讨论在内体生物发生和成熟的背景下酵母和后生动物细胞中两种复合物的一般功能。
Protein and lipid transport along the endolysosomal system of eukaryotic cells depends on multiple fusion and fission events. Over the past few years, the molecular constituents of both fission and fusion machineries have been identified. Here, we focus on the mechanism of membrane fusion at endosomes, vacuoles and lysosomes, and in particular on the role of the two homologous tethering complexes called CORVET and HOPS. Both complexes are heterohexamers; they share four subunits, interact with Rab GTPases and soluble NSF attachment protein receptors (SNAREs) and can tether membranes. Owing to the presence of specific subunits, CORVET is a Rab5 effector complex, whereas HOPS can bind efficiently to late endosomes and lysosomes through Rab7. Based on the recently described overall structure of the HOPS complex and a number of in vivo and in vitro analyses, important insights into their function have been obtained. Here, we discuss the general function of both complexes in yeast and in metazoan cells in the context of endosomal biogenesis and maturation.