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Title: A role for Vps13-mediated lipid transfer at the ER-endosome contact site in ESCRT-mediated sorting
Authors: Suzuki, Sho W.
West, Matthew
Zhang, Yichen
Fan, Jenny S.
Roberts, Rachel T.
Odorizzi, Greg
Emr, Scott D.
Keywords: Medicine, Health and Life Sciences
Issue Date: 2024
Source: Suzuki, S. W., West, M., Zhang, Y., Fan, J. S., Roberts, R. T., Odorizzi, G. & Emr, S. D. (2024). A role for Vps13-mediated lipid transfer at the ER-endosome contact site in ESCRT-mediated sorting. Journal of Cell Biology, 223(4), e202307094-.
Journal: Journal of Cell Biology 
Abstract: Endosomes are specialized organelles that function in the secretory and endocytic protein sorting pathways. Endocytosed cell surface receptors and transporters destined for lysosomal degradation are sorted into intraluminal vesicles (ILVs) at endosomes by endosomal sorting complexes required for transport (ESCRT) proteins. The endosomes (multivesicular bodies, MVBs) then fuse with the lysosome. During endosomal maturation, the number of ILVs increases, but the size of endosomes does not decrease despite the consumption of the limiting membrane during ILV formation. Vesicle-mediated trafficking is thought to provide lipids to support MVB biogenesis. However, we have uncovered an unexpected contribution of a large bridge-like lipid transfer protein, Vps13, in this process. Here, we reveal that Vps13-mediated lipid transfer at ER-endosome contact sites is required for the ESCRT pathway. We propose that Vps13 may play a critical role in supplying lipids to the endosome, ensuring continuous ESCRT-mediated sorting during MVB biogenesis.
ISSN: 0021-9525
DOI: 10.1083/jcb.202307094
Schools: School of Biological Sciences 
Rights: © 2024 Suzuki et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at
Fulltext Permission: open
Fulltext Availability: With Fulltext
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