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TitleThree-dimensional architecture of ESCRT-III flat spirals on the membrane.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 20, Page e2319115121, Year 2024
Publish dateMay 14, 2024
AuthorsMingdong Liu / Yunhui Liu / Tiefeng Song / Liuyan Yang / Lei Qi / Yu-Zhong Zhang / Yong Wang / Qing-Tao Shen /
PubMed AbstractThe endosomal sorting complexes required for transport (ESCRTs) are responsible for membrane remodeling in many cellular processes, such as multivesicular body biogenesis, viral budding, and ...The endosomal sorting complexes required for transport (ESCRTs) are responsible for membrane remodeling in many cellular processes, such as multivesicular body biogenesis, viral budding, and cytokinetic abscission. ESCRT-III, the most abundant ESCRT subunit, assembles into flat spirals as the primed state, essential to initiate membrane invagination. However, the three-dimensional architecture of ESCRT-III flat spirals remained vague for decades due to highly curved filaments with a small diameter and a single preferred orientation on the membrane. Here, we unveiled that yeast Snf7, a component of ESCRT-III, forms flat spirals on the lipid monolayers using cryogenic electron microscopy. We developed a geometry-constrained Euler angle-assigned reconstruction strategy and obtained moderate-resolution structures of Snf7 flat spirals with varying curvatures. Our analyses showed that Snf7 subunits recline on the membrane with N-terminal motifs α0 as anchors, adopt an open state with fused α2/3 helices, and bend α2/3 gradually from the outer to inner parts of flat spirals. In all, we provide the orientation and conformations of ESCRT-III flat spirals on the membrane and unveil the underlying assembly mechanism, which will serve as the initial step in understanding how ESCRTs drive membrane abscission.
External linksProc Natl Acad Sci U S A / PubMed:38709931 / PubMed Central
MethodsEM (single particle)
Resolution7.1 - 7.4 Å
Structure data

37416

8wb6

EMDB-37416, PDB-8wb6:
Cryo-EM structure of Snf7 N-terminal domain in outer coils of spiral polymers
Method: EM (single particle) / Resolution: 7.1 Å

37417

8wb7

EMDB-37417, PDB-8wb7:
CryoEM structure of Snf7 N-terminal domain in the inner coils of spiral
Method: EM (single particle) / Resolution: 7.4 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsPROTEIN TRANSPORT / membrane fission / spiral polymers / N-terminal domain / "open" status

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