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8AFZ

Architecture of the ESCPE-1 membrane coat

Summary for 8AFZ
Entry DOI10.2210/pdb8afz/pdb
EMDB information15413
DescriptorSorting nexin-1, Sorting nexin-5, Cation-independent mannose-6-phosphate receptor (3 entities in total)
Functional Keywordssorting nexins, px domain, bar domain, endosomes, retrograde transport, endocytic recycling, cargo recognition, protein coat, membrane recruitment, membrane deformation, membrane tubules., transport protein
Biological sourceHomo sapiens (human)
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Total number of polymer chains3
Total formula weight109801.88
Authors
Primary citationLopez-Robles, C.,Scaramuzza, S.,Astorga-Simon, E.N.,Ishida, M.,Williamson, C.D.,Banos-Mateos, S.,Gil-Carton, D.,Romero-Durana, M.,Vidaurrazaga, A.,Fernandez-Recio, J.,Rojas, A.L.,Bonifacino, J.S.,Castano-Diez, D.,Hierro, A.
Architecture of the ESCPE-1 membrane coat.
Nat.Struct.Mol.Biol., 30:958-969, 2023
Cited by
PubMed Abstract: Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1), which rescues transmembrane proteins from the endolysosomal pathway for transport to the trans-Golgi network and the plasma membrane. This rescue entails the formation of recycling tubules through ESCPE-1 recruitment, cargo capture, coat assembly and membrane sculpting by mechanisms that remain largely unknown. Herein, we show that ESCPE-1 has a single-layer coat organization and suggest how synergistic interactions between ESCPE-1 protomers, phosphoinositides and cargo molecules result in a global arrangement of amphipathic helices to drive tubule formation. Our results thus define a key process of tubule-based endosomal sorting.
PubMed: 37322239
DOI: 10.1038/s41594-023-01014-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (10 Å)
Structure validation

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