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SHIP164 is a Chorein Motif Containing Lipid Transport Protein that Controls Membrane Dynamics and Traffic at the Endosome-Golgi Interface
Open accessPreprint — published as 10.1083/jcb.202111018 · Paper page
Abstract
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.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Hanna, M. G., Suen, P., Wu, Y., Reinisch, K. M., & De Camilli, P.
- Affiliations
- Howard Hughes Medical Institute (US)
- Yale University (US)
- Venue
- The Journal of Cell Biology
- Publisher
- openRxiv
- Published
- 2021-11-04
- Volume
- 221
- Issue
- 6
- ISSN
- 0021-9525 (ISSN-L)
- PMC
- PMC9067936
- OpenAlex
- W4225282945
- Cited by
- 39
- References
- 1
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 7 · 2023: 5 · 2022: 10
- FWCI
- 4.14
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Michael J. Fox Foundation for Parkinson's Research (ASAP-000580)
- National Parkinson Foundation
- Parkinson's Foundation
- Aligning Science Across Parkinson’s (ASAP-000580)
- National Institutes of Health (NS36251, DK-45735, DA18343)
- Parkinsonfonden (ASAP-000580)
- National Institute on Drug Abuse (P30DA018343)
- National Institute of General Medical Sciences (T32GM008283, R35GM131715)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30DK045735)
- National Institute of Neurological Disorders and Stroke (F32NS108448, R01NS036251, R37NS036251)
- Kavli Institute for Neuroscience, Yale School of Medicine
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Keywords
- lipid transfer proteins, retrograde transport, cation-independent mannose 6-phosphate receptor, membrane contact sites, membrane lipid composition
- MeSH terms
- Carrier Proteins, Golgi Apparatus, Intracellular Membranes, Lipids, Endosomes, Intracellular Signaling Peptides and Proteins
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