Publications
Resources / Publications
Michael G. Hanna (1,2,3,4), Patreece Suen (2), Yumei Wu (1,2,3,4), Karin M. Reinisch (2,6), Pietro De Camilli (1,2,3,4,5,6)
bioRxiv, November 2021. DOI: 10.1101/2021.11.04.467353
Cellular membranes differ in protein and lipid composition as well as in the protein-lipid ratio. Thus, progression of membranous organelles along traffic routes requires mechanisms to control bilayer lipid chemistry and their abundance relative to proteins. The recent structural and functional characterization of VPS13-family proteins has suggested a mechanism through which lipids can be transferred in bulk from one membrane to another at membrane contact sites, and thus independently of vesicular traffic. Here we show that SHIP164 (UHRF1BP1L) shares structural and lipid transfer properties with these proteins and is localized on a subpopulation of vesicle clusters in the early endocytic pathway whose membrane cargo includes the cation-independent mannose-6-phosphate receptor (MPR) and ATG9. Loss of SHIP164 disrupts retrograde traffic of these organelles to the Golgi complex. Our findings raise the possibility that bulk transfer of lipids to endocytic membranes may play a role in their traffic.
Dragonfly was used to process and analyse FIB-SEM data.
(1) Department of Neuroscience, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
(2) Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
(3) Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
(4) Program in Cellular Neuroscience, Neurodegeneration and Repair, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
(5) Kavli Institue for Neuroscience, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
(6)Aligning Science Across Parkinson’s (ASAP) Collaborative Research Network, Chevy Chase, MD.
Return to Publications list.
We'd be pleased to add your paper to our publications list.