8qx8
From Proteopedia
Endosomal membrane tethering complex CORVET
Structural highlights
FunctionVPS8_YEAST Required for localization and recycling of the CPY sorting receptor (VPS10) to the late-Golgi compartment. Involved in the retention of proteins to the late-Golgi. Plays an integral role in the complex vacuolar protein sorting process. Publication Abstract from PubMedCells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion steps. Early endosome fusion is promoted by the Rab5 GTPase and its effector, the hexameric CORVET tethering complex, which is homologous to the lysosomal HOPS. How these related complexes recognize their specific target membranes remains entirely elusive. Here, we solve the structure of CORVET by cryo-electron microscopy and revealed its minimal requirements for membrane tethering. As expected, the core of CORVET and HOPS resembles each other. However, the function-defining subunits show marked structural differences. Notably, we discover that unlike HOPS, CORVET depends not only on Rab5 but also on phosphatidylinositol-3-phosphate (PI3P) and membrane lipid packing defects for tethering, implying that an organelle-specific membrane code enables fusion. Our data suggest that both shape and membrane interactions of CORVET and HOPS are conserved in metazoans, thus providing a paradigm how tethering complexes function. Structure of the endosomal CORVET tethering complex.,Shvarev D, Konig C, Susan N, Langemeyer L, Walter S, Perz A, Frohlich F, Ungermann C, Moeller A Nat Commun. 2024 Jun 19;15(1):5227. doi: 10.1038/s41467-024-49137-9. PMID:38898033[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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