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The mechanisms of these diseases are unknown. Genetic studies in yeast hinted that Vps13 may have a role in lipid exchange between organelles. In this study, we show that the N-terminal portion of VPS13 is tubular, with a hydrophobic cavity that can solubilize and transport glycerolipids between membranes. We also show that human VPS13A and VPS13C bind to the ER, tethering it to mitochondria (VPS13A), to late endosome\/lysosomes (VPS13C), and to lipid droplets (both VPS13A and VPS13C). These findings identify VPS13 as a lipid transporter between the ER and other organelles, implicating defects in membrane lipid homeostasis in neurological disorders resulting from their mutations. Sequence and secondary structure similarity between the N-terminal portions of Vps13 and other proteins such as the autophagy protein ATG2 suggest lipid transport roles for these proteins as well.<\/jats:p>","DOI":"10.1083\/jcb.201807019","type":"journal-article","created":{"date-parts":[[2018,8,9]],"date-time":"2018-08-09T11:30:50Z","timestamp":1533814250000},"page":"3625-3639","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":628,"title":["VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites"],"prefix":"10.1083","volume":"217","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3673-2302","authenticated-orcid":true,"given":"Nikit","family":"Kumar","sequence":"first","affiliation":[{"name":"Department of Cell Biology, Yale University School of Medicine, New Haven, CT 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