Kinesin 1 Drives Autolysosome Tubulation

Wanqing Du; Qian Peter Su; Yang Chen; Yueyao Zhu; Dong Jiang; Yueguang Rong; Senyan Zhang; Yixiao Zhang; He Ren; Chuanmao Zhang; Xinquan Wang; Ning Gao; Yanfeng Wang; Lingfei Sun; Yujie Sun; Li Yu

doi:10.1016/j.devcel.2016.04.014

Kinesin 1 Drives Autolysosome Tubulation

Wanqing Du, Qian Peter Su, Yang Chen, Yueyao Zhu, Dong Jiang, Yueguang Rong, Senyan Zhang, Yixiao Zhang, He Ren, Chuanmao Zhang, Xinquan Wang, Ning Gao, Yanfeng Wang, Lingfei Sun, Yujie Sun, Li Yu

Research output: Contribution to journal › Article › peer-review

106 Scopus citations

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.

Original language	English (US)
Pages (from-to)	326-336
Number of pages	11
Journal	Developmental cell
Volume	37
Issue number	4
DOIs	https://doi.org/10.1016/j.devcel.2016.04.014
State	Published - May 23 2016
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
General Biochemistry, Genetics and Molecular Biology
Developmental Biology
Cell Biology

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10.1016/j.devcel.2016.04.014

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@article{da90da474a7944e281ac88d4cddc945a,

title = "Kinesin 1 Drives Autolysosome Tubulation",

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.",

author = "Wanqing Du and Su, {Qian Peter} and Yang Chen and Yueyao Zhu and Dong Jiang and Yueguang Rong and Senyan Zhang and Yixiao Zhang and He Ren and Chuanmao Zhang and Xinquan Wang and Ning Gao and Yanfeng Wang and Lingfei Sun and Yujie Sun and Li Yu",

note = "Funding Information: We are grateful to Nikon Instruments (Shanghai) and the Tsinghua Cell Biology Core Facility for providing technical support. This research was supported by the National Natural Science Foundation of China 31430053 and 31321003 , Natural Science Foundation of China international cooperation and exchange program 31561143002 , Beijing Natural Science Foundation 5142011 , International Cooperation Grant of Science and Technology 2014DFG32460 , National Science Foundation of China 21573013 , 21390412 , 31271423 , and 31327901 , 863 Program SS2015AA020406 , and CAS Interdisciplinary Innovation Team for Y.S. Publisher Copyright: {\textcopyright} 2016 Elsevier Inc.",

year = "2016",

month = may,

day = "23",

doi = "10.1016/j.devcel.2016.04.014",

language = "English (US)",

volume = "37",

pages = "326--336",

journal = "Developmental cell",

issn = "1534-5807",

publisher = "Cell Press",

number = "4",

}

TY - JOUR

T1 - Kinesin 1 Drives Autolysosome Tubulation

AU - Du, Wanqing

AU - Su, Qian Peter

AU - Chen, Yang

AU - Zhu, Yueyao

AU - Jiang, Dong

AU - Rong, Yueguang

AU - Zhang, Senyan

AU - Zhang, Yixiao

AU - Ren, He

AU - Zhang, Chuanmao

AU - Wang, Xinquan

AU - Gao, Ning

AU - Wang, Yanfeng

AU - Sun, Lingfei

AU - Sun, Yujie

AU - Yu, Li

N1 - Funding Information: We are grateful to Nikon Instruments (Shanghai) and the Tsinghua Cell Biology Core Facility for providing technical support. This research was supported by the National Natural Science Foundation of China 31430053 and 31321003 , Natural Science Foundation of China international cooperation and exchange program 31561143002 , Beijing Natural Science Foundation 5142011 , International Cooperation Grant of Science and Technology 2014DFG32460 , National Science Foundation of China 21573013 , 21390412 , 31271423 , and 31327901 , 863 Program SS2015AA020406 , and CAS Interdisciplinary Innovation Team for Y.S. Publisher Copyright: © 2016 Elsevier Inc.

PY - 2016/5/23

Y1 - 2016/5/23

N2 - 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.

AB - 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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U2 - 10.1016/j.devcel.2016.04.014

DO - 10.1016/j.devcel.2016.04.014

M3 - Article

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AN - SCOPUS:84969706548

SN - 1534-5807

VL - 37

SP - 326

EP - 336

JO - Developmental cell

JF - Developmental cell

IS - 4

ER -

Kinesin 1 Drives Autolysosome Tubulation

Abstract

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