Kinesin 1 Drives Autolysosome Tubulation

Du, W; Su, QP; Chen, Y; Zhu, Y; Jiang, D; Rong, Y; Zhang, S; Zhang, Y; Ren, H; Zhang, C; Wang, X; Gao, N; Wang, Y; Sun, L; Sun, Y; Yu, L

Kinesin 1 Drives Autolysosome Tubulation

Du, W Su, QP

Chen, Y Zhu, Y Jiang, D Rong, Y Zhang, S Zhang, Y Ren, H Zhang, C Wang, X Gao, N Wang, Y Sun, L Sun, Y Yu, L

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Publication Type:: Journal Article
Citation:: Developmental Cell, 2016, 37 (4), pp. 326 - 336
Issue Date:: 2016-05-23

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Field	Value	Language
dc.contributor.author	Du, W	en_US
dc.contributor.author	Su, QP https://orcid.org/0000-0001-7364-3945	en_US
dc.contributor.author	Chen, Y	en_US
dc.contributor.author	Zhu, Y	en_US
dc.contributor.author	Jiang, D	en_US
dc.contributor.author	Rong, Y	en_US
dc.contributor.author	Zhang, S	en_US
dc.contributor.author	Zhang, Y	en_US
dc.contributor.author	Ren, H	en_US
dc.contributor.author	Zhang, C	en_US
dc.contributor.author	Wang, X	en_US
dc.contributor.author	Gao, N	en_US
dc.contributor.author	Wang, Y	en_US
dc.contributor.author	Sun, L	en_US
dc.contributor.author	Sun, Y	en_US
dc.contributor.author	Yu, L	en_US
dc.date.available	2016-04-20	en_US
dc.date.issued	2016-05-23	en_US
dc.identifier.citation	Developmental Cell, 2016, 37 (4), pp. 326 - 336	en_US
dc.identifier.issn	1534-5807	en_US
dc.identifier.uri	http://hdl.handle.net/10453/118495
dc.description.abstract	© 2016 Elsevier Inc. 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.	en_US
dc.relation.ispartof	Developmental Cell	en_US
dc.relation.isbasedon	10.1016/j.devcel.2016.04.014	en_US
dc.subject.classification	Developmental Biology	en_US
dc.subject.mesh	Membrane Microdomains	en_US
dc.subject.mesh	Lysosomes	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Rats	en_US
dc.subject.mesh	Kinesin	en_US
dc.subject.mesh	Phosphatidylinositol 4,5-Diphosphate	en_US
dc.subject.mesh	Clathrin	en_US
dc.subject.mesh	Liposomes	en_US
dc.subject.mesh	Models, Biological	en_US
dc.subject.mesh	Autophagy	en_US
dc.title	Kinesin 1 Drives Autolysosome Tubulation	en_US
dc.type	Journal Article
utslib.citation.volume	4	en_US
utslib.citation.volume	37	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Mathematical and Physical Sciences
utslib.copyright.status	closed_access
pubs.issue	4	en_US
pubs.publication-status	Published	en_US
pubs.volume	37	en_US

Abstract:

© 2016 Elsevier Inc. 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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http://hdl.handle.net/10453/118495