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| Open AccessSiglec-6 mediates the uptake of extracellular vesicles through a noncanonical glycolipid binding pocket
Siglec-glycolipid interactions are often studied outside the context of a lipid bilayer. Here, the authors combine a variety of chemical biology techniques to demonstrate a unique and physiologically relevant ability of Siglec-6 to recognize glycolipids in a membrane.
- Edward N. Schmidt
- , Dimitra Lamprinaki
- & Matthew S. Macauley
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Article
| Open AccessGlycolysis regulates KRAS plasma membrane localization and function through defined glycosphingolipids
KRAS is a small GTPase that regulates cell proliferation. Here, the authors show that a subset of cell surface glycosphingolipids regulate KRAS plasma membrane localization by modulating inner leaflet lipid composition, uncovering a requirement for KRAS oncogenesis that may have therapeutic potential.
- Junchen Liu
- , Ransome van der Hoeven
- & John F. Hancock
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Article
| Open AccessDeficiency of the frontotemporal dementia gene GRN results in gangliosidosis
Progranulin-deficieny results in gangliosidosis due to reduced lysosomal lipids (BMP) required for ganglioside degradation. Lysosomal ganglioside accumulation may contribute to neuroinflammation and neurodegeneration susceptibility observed in FTD.
- Sebastian Boland
- , Sharan Swarup
- & Robert V. Farese Jr
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Article
| Open AccessUnravelling the structural complexity of glycolipids with cryogenic infrared spectroscopy
Glycolipids are glycoconjugates with important biological functions, but techniques for their analysis are deficient. Here, the authors report the use of cryogenic gas-phase infrared spectroscopy to investigate isomerism in a set of immunologically relevant glycolipids, and show that their structural features can be accurately resolved based on a narrow spectral fingerprint region.
- Carla Kirschbaum
- , Kim Greis
- & Kevin Pagel
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Article
| Open AccessCross-talks of glycosylphosphatidylinositol biosynthesis with glycosphingolipid biosynthesis and ER-associated degradation
Glycosylphosphatidylinositol (GPI) anchors are found on many cell surface proteins but their biosynthesis is not fully understood. Here, the authors identify genes involved in GPI galactosylation and reveal functional connections between GPI processing, glycosphingolipid biosynthesis and ER-associated degradation.
- Yicheng Wang
- , Yusuke Maeda
- & Taroh Kinoshita
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Article
| Open AccessIdentification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain
Mammalian GPI membrane anchors are modified by GalNAc to confer structural diversity but the biosynthetic pathway is poorly understood. Here, the authors identify and characterize the Golgi-resident GPI-GalNAc transferase PGAP4, providing insights into the initial step of GPI-GalNAc biosynthesis.
- Tetsuya Hirata
- , Sushil K. Mishra
- & Taroh Kinoshita
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Article
| Open AccessStructural basis for dolichylphosphate mannose biosynthesis
The generation of glycolipid dolichylphosphate mannose (Dol-P-Man) is a critical step for protein glycosylation and GPI anchor synthesis. Here the authors report the structure of dolichylphosphate mannose synthase in complex with bound nucleotide and donor to provide insight into the mechanism of Dol-P-Man synthesis.
- Rosaria Gandini
- , Tom Reichenbach
- & Christina Divne
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Article
| Open AccessDynamic caveolae exclude bulk membrane proteins and are required for sorting of excess glycosphingolipids
Recent data question the long-assumed link between caveolae and endocytosis of membrane proteins. Shvets et al. use genome editing to tag and trace endogenous caveolar proteins, providing evidence that these structures exclude membrane proteins and are instead required for proper sorting of excess membrane lipids.
- Elena Shvets
- , Vassilis Bitsikas
- & Benjamin J. Nichols
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Article
| Open AccessMPIase is a glycolipozyme essential for membrane protein integration
Proteins are integrated into cellular membranes either co-translationally through Sec/SRP or post-translationally by chaperones. These authors show that an integration-dedicated chaperone inE. coli, MPIase, is a glycolipid and facilitates protein insertion into the inner membrane of the bacterium.
- Ken-ichi Nishiyama
- , Masahide Maeda
- & Keiko Shimamoto