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Atg8 同源物作为信号转导支架的可能作用。

A possible role of Atg8 homologs as a scaffold for signal transduction.

机构信息

Department of Developmental Biology and Neurosciences, Graduate School of Life Sciences, Tohoku University, Sendai, Miyagi, Japan.

出版信息

Autophagy. 2011 Sep;7(9):1080-1. doi: 10.4161/auto.7.9.16178. Epub 2011 Sep 1.

Abstract

Atg8 and its homologs are essential for autophagosome formation in various species. In animal cells, Atg8 homologs have an additional function in clearance of damaged organelles and bacteria, acting as a landmark for selective autophagy. We have recently shown that OATL1, a Rab-GTPase-activating protein (Rab-GAP), is a novel binding partner of Atg8 homologs in mammalian cells, but to our surprise, it is not a substrate of autophagy. Further analysis indicates that OATL1 is involved in the fusion between autophagosomes and lysosomes through its GAP activity and its Atg8 homolog binding activity. Our findings suggest a novel function of Atg8 homologs as a scaffold for signal transduction that regulates autophagosomal maturation.

摘要

Atg8 及其同源物对于各种物种的自噬体形成是必不可少的。在动物细胞中,Atg8 同源物在清除受损细胞器和细菌方面具有额外的功能,作为选择性自噬的标志物。我们最近表明,Rab-GTPase 激活蛋白 (Rab-GAP) OATL1 是哺乳动物细胞中 Atg8 同源物的新型结合伴侣,但令我们惊讶的是,它不是自噬的底物。进一步的分析表明,OATL1 通过其 GAP 活性和 Atg8 同源物结合活性参与自噬体与溶酶体之间的融合。我们的发现表明 Atg8 同源物作为一种信号转导支架的新功能,调节自噬体的成熟。

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