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. 2016 May 23;37(4):326-336.
doi: 10.1016/j.devcel.2016.04.014.

Kinesin 1 Drives Autolysosome Tubulation

Wanqing Du  1 , Qian Peter Su  2 , Yang Chen  3 , Yueyao Zhu  3 , Dong Jiang  3 , Yueguang Rong  3 , Senyan Zhang  3 , Yixiao Zhang  3 , He Ren  4 , Chuanmao Zhang  4 , Xinquan Wang  5 , Ning Gao  5 , Yanfeng Wang  5 , Lingfei Sun  5 , Yujie Sun  6 , Li Yu  7
Affiliations
Free article

Kinesin 1 Drives Autolysosome Tubulation

Wanqing Du et al. Dev Cell. .
Free article

Abstract

Autophagic lysosome reformation (ALR) plays an important role in maintaining lysosome homeostasis. During ALR, lysosomes are reformed by recycling lysosomal components from autolysosomes. The most noticeable step of ALR is autolysosome tubulation, but it is currently unknown how the process is regulated. Here, using an approach combining in vivo studies and in vitro reconstitution, we found that the kinesin motor protein KIF5B is required for autolysosome tubulation and that KIF5B drives autolysosome tubulation by pulling on the autolysosomal membrane. Furthermore, we show that KIF5B directly interacts with PtdIns(4,5)P2. Kinesin motors are recruited and clustered on autolysosomes via interaction with PtdIns(4,5)P2 in a clathrin-dependent manner. Finally, we demonstrate that clathrin promotes formation of PtdIns(4,5)P2-enriched microdomains, which are required for clustering of KIF5B. Our study reveals a mechanism by which autolysosome tubulation was generated.

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