Molecular Cancer Research Group, Institute of Medical Biology, University of Tromsø, 9037 Tromsø, Norway.
J Cell Biol. 2010 Jan 25;188(2):253-69. doi: 10.1083/jcb.200907015.
Autophagy is the main eukaryotic degradation pathway for long-lived proteins, protein aggregates, and cytosolic organelles. Although the protein machinery involved in the biogenesis of autophagic vesicles is well described, very little is known about the mechanism of cytosolic transport of autophagosomes. In this study, we have identified an adaptor protein complex, formed by the two autophagic membrane-associated proteins LC3 and Rab7 and the novel FYVE and coiled-coil (CC) domain-containing protein FYCO1, that promotes microtubule (MT) plus end-directed transport of autophagic vesicles. We have characterized the LC3-, Rab7-, and phosphatidylinositol-3-phosphate-binding domains in FYCO1 and mapped part of the CC region essential for MT plus end-directed transport. We also propose a mechanism for selective autophagosomal membrane recruitment of FYCO1.
自噬是长寿命蛋白、蛋白质聚集体和细胞质细胞器的主要真核降解途径。尽管参与自噬小体生物发生的蛋白质机制已经得到很好的描述，但对于细胞质中自噬体的运输机制知之甚少。在这项研究中，我们已经鉴定出一种衔接蛋白复合物，由两种自噬膜相关蛋白 LC3 和 Rab7 以及新型 FYVE 和卷曲螺旋（CC）结构域蛋白 FYCO1 组成，它促进自噬小体的微管（MT）正极定向运输。我们已经鉴定了 FYCO1 中与 LC3、Rab7 和磷脂酰肌醇-3-磷酸结合的结构域，并绘制了 CC 区域的一部分，该区域对于 MT 正极定向运输是必需的。我们还提出了 FYCO1 对选择性自噬体膜募集的机制。
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