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
- Publication Type:
- Journal Article
- Citation:
- Developmental Cell, 2016, 37 (4), pp. 326 - 336
- Issue Date:
- 2016-05-23
Closed Access
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1-s2.0-S1534580716302349-main.pdf | Published Version | 3.06 MB |
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Full metadata record
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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