TRAF6 mediates ubiquitination of KIF23/MKLP1 and is required for midbody ring degradation by selective autophagy
TRAF6 mediates ubiquitination of KIF23/MKLP1 and is required for midbody ring degradation by selective autophagy
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DOI：
10.4161/auto.26085
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发表时间：
2013-12-01
期刊：
影响因子：
13.3
通讯作者：
Simonsen, Anne
中科院分区：
文献类型：
--
作者：
Isakson, Pauline;Lystad, Alf Hakon;Simonsen, Anne
在细胞质分裂完成后，中体环被不对称地输送到两个子细胞中的一个，在那里它成为被自噬降解的中体环衍生物。在这项研究中，我们证明了泛素结合的自噬受体SQSTM1/p62和相互作用的接头蛋白WDFY3/Alfy与泛素E3连接酶TRAF6形成一个复合体，这些蛋白以及NBR1对于自噬有效地清除中体环衍生物是重要的。在TRAF6缺失的细胞中，泛素化的中体环衍生物的数量减少，我们发现TRAF6介导了中体环定位蛋白KIF23/MKLP1的泛素化。我们得出结论，TRAF6介导的中体环的泛素化对于其随后被泛素结合的自噬受体识别和选择性自噬降解是重要的。
Upon completion of cytokinesis, the midbody ring is transported asymmetrically into one of the two daughter cells where it becomes a midbody ring derivative that is degraded by autophagy. In this study we showed that the ubiquitin-binding autophagy receptor SQSTM1/p62 and the interacting adaptor protein WDFY3/ALFY form a complex with the ubiquitin E3 ligase TRAF6 and that these proteins, as well as NBR1, are important for efficient clearance of midbody ring derivatives by autophagy. The number of ubiquitinated midbody ring derivatives decreases in TRAF6-depleted cells and we showed that TRAF6 mediates ubiquitination of the midbody ring localized protein KIF23/MKLP1. We conclude that TRAF6-mediated ubiquitination of the midbody ring is important for its subsequent recognition by ubiquitin-binding autophagy receptors and degradation by selective autophagy.