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TitleImproved mammalian retromer cryo-EM structures reveal a new assembly interface.
Journal, issue, pagesJ Biol Chem, Vol. 298, Issue 11, Page 102523, Year 2022
Publish dateSep 26, 2022
AuthorsAmy K Kendall / Mintu Chandra / Boyang Xie / William Wan / Lauren P Jackson /
PubMed AbstractRetromer (VPS26/VPS35/VPS29 subunits) assembles with multiple sorting nexin proteins on membranes to mediate endosomal recycling of transmembrane protein cargoes. Retromer has been implicated in ...Retromer (VPS26/VPS35/VPS29 subunits) assembles with multiple sorting nexin proteins on membranes to mediate endosomal recycling of transmembrane protein cargoes. Retromer has been implicated in other cellular processes, including mitochondrial homeostasis, nutrient sensing, autophagy, and fission events. Mechanisms for mammalian retromer assembly remain undefined, and retromer engages multiple sorting nexin proteins to sort cargoes to different destinations. Published structures demonstrate mammalian retromer forms oligomers in vitro, but several structures were poorly resolved. We report here improved retromer oligomer structures using single-particle cryo-EM by combining data collected from tilted specimens with multiple advancements in data processing, including using a 3D starting model for enhanced automated particle picking in RELION. We used a retromer mutant (3KE retromer) that breaks VPS35-mediated interfaces to determine a structure of a new assembly interface formed by the VPS26A and VPS35 N-termini. The interface reveals how an N-terminal VPS26A arrestin saddle can link retromer chains by engaging a neighboring VPS35 N- terminus, on the opposite side from the well-characterized C-VPS26/N-VPS35 interaction observed within heterotrimers. The new interaction interface exhibits substantial buried surface area (∼7000 Å) and further suggests that metazoan retromer may serve as an adaptable scaffold.
External linksJ Biol Chem / PubMed:36174678 / PubMed Central
MethodsEM (single particle)
Resolution4.5 - 7.3 Å
Structure data

EMDB-26340: Mouse retromer (VPS26/VPS35 E615A/D616A/E617A mutant/VPS29) 3KE particle sub-structure
Method: EM (single particle) / Resolution: 7.2 Å

EMDB-26341: Mouse retromer (VPS26/VPS35 E615A/D616A/E617A mutant/VPS29) 3KE particle
Method: EM (single particle) / Resolution: 7.1 Å

EMDB-26342: Mouse retromer (VPS26/VPS35/VPS29) dimer of heterotrimers
Method: EM (single particle) / Resolution: 7.0 Å

EMDB-26343: Mouse retromer sub-structure: VPS35/VPS35 curved dimer
Method: EM (single particle) / Resolution: 7.3 Å

EMDB-26345: Mouse retromer sub-structure: VPS35/VPS35 flat substructure
Method: EM (single particle) / Resolution: 4.5 Å

PDB-7u6f:
Mouse retromer (VPS26/VPS35/VPS29) heterotrimers
Method: ELECTRON MICROSCOPY / Resolution: 4.9 Å

Chemicals

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-EDO:
1,2-ETHANEDIOL / Ethylene glycol

ChemComp-HOH:
WATER / Water

Source
  • mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN / retromer / membrane trafficking / endosomal trafficking / membrane coat complexes / PROTEIN TRANSPORT

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