An ESCRT-dependent step in fatty acid transfer from lipid droplets to mitochondria through VPS13D−TSG101 interactions DOI Creative Commons
Jingru Wang, Na Fang, Juan Xiong

et al.

Nature Communications, Journal Year: 2021, Volume and Issue: 12(1)

Published: Feb. 23, 2021

Abstract Upon starvation, cells rewire their metabolism, switching from glucose-based metabolism to mitochondrial oxidation of fatty acids, which require the transfer FAs lipid droplets (LDs) mitochondria at mitochondria−LD membrane contact sites (MCSs). However, factors responsible for FA these MCSs remain uncharacterized. Here, we demonstrate that vacuolar protein sorting-associated 13D (VPS13D), loss-of-function mutations cause spastic ataxia, coordinates trafficking in conjunction with endosomal sorting complex required transport (ESCRT) tumor susceptibility 101 (TSG101). The VPS13 adaptor-binding domain VPS13D and TSG101 directly remodels LD membranes a cooperative manner. human binds glycerophospholipids vitro. Depletion VPS13D, TSG101, or ESCRT-III proteins inhibits LDs mitochondria. Our findings suggest mediates ESCRT-dependent remodeling facilitate mitochondria-LD contacts.

Language: Английский

Lysosomal dysfunction in neurodegeneration: emerging concepts and methods DOI Creative Commons
Vinod Udayar, Yu Chen, Ellen Sidransky

et al.

Trends in Neurosciences, Journal Year: 2022, Volume and Issue: 45(3), P. 184 - 199

Published: Jan. 13, 2022

Language: Английский

Citations

135
Lipid Droplet Contact Sites in Health and Disease DOI
Eva Herker, Gabrielle Vièyres, Mathias Beller

et al.

Trends in Cell Biology, Journal Year: 2021, Volume and Issue: 31(5), P. 345 - 358

Published: Feb. 3, 2021

Language: Английский

Citations

130
Mechanisms of nonvesicular lipid transport DOI Creative Commons
Karin M. Reinisch, William A. Prinz

The Journal of Cell Biology, Journal Year: 2021, Volume and Issue: 220(3)

Published: Feb. 19, 2021

We have long known that lipids traffic between cellular membranes via vesicles but only recently appreciated the role of nonvesicular lipid transport. Nonvesicular transport can be high volume, supporting biogenesis rapidly expanding membranes, or more targeted and precise, allowing cells to alter levels specific in membranes. Most such probably occurs at membrane contact sites, where organelles are closely apposed, requires proteins (LTPs), which solubilize shield them from aqueous phase during their Some LTPs cup like shuttle monomers Others form conduits flow This review describes what we know about transfer mechanisms while also identifying many remaining unknowns: How do facilitate movement into require accessory for efficient vivo, how is directionality determined?

Language: Английский

Citations

129
Regulation of phospholipid distribution in the lipid bilayer by flippases and scramblases DOI Open Access
Takaharu Sakuragi, Shigekazu Nagata

Nature Reviews Molecular Cell Biology, Journal Year: 2023, Volume and Issue: 24(8), P. 576 - 596

Published: April 27, 2023

Language: Английский

Citations

123
An ESCRT-dependent step in fatty acid transfer from lipid droplets to mitochondria through VPS13D−TSG101 interactions DOI Creative Commons
Jingru Wang, Na Fang, Juan Xiong

et al.

Nature Communications, Journal Year: 2021, Volume and Issue: 12(1)

Published: Feb. 23, 2021

Abstract Upon starvation, cells rewire their metabolism, switching from glucose-based metabolism to mitochondrial oxidation of fatty acids, which require the transfer FAs lipid droplets (LDs) mitochondria at mitochondria−LD membrane contact sites (MCSs). However, factors responsible for FA these MCSs remain uncharacterized. Here, we demonstrate that vacuolar protein sorting-associated 13D (VPS13D), loss-of-function mutations cause spastic ataxia, coordinates trafficking in conjunction with endosomal sorting complex required transport (ESCRT) tumor susceptibility 101 (TSG101). The VPS13 adaptor-binding domain VPS13D and TSG101 directly remodels LD membranes a cooperative manner. human binds glycerophospholipids vitro. Depletion VPS13D, TSG101, or ESCRT-III proteins inhibits LDs mitochondria. Our findings suggest mediates ESCRT-dependent remodeling facilitate mitochondria-LD contacts.

Language: Английский

Citations

109