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TitleMolecular architecture of the human caveolin-1 complex.
Journal, issue, pagesSci Adv, Vol. 8, Issue 19, Page eabn7232, Year 2022
Publish dateMay 13, 2022
AuthorsJason C Porta / Bing Han / Alican Gulsevin / Jeong Min Chung / Yelena Peskova / Sarah Connolly / Hassane S Mchaourab / Jens Meiler / Erkan Karakas / Anne K Kenworthy / Melanie D Ohi /
PubMed AbstractMembrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin ...Membrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin function as essential curvature-generating components of caveolae, flask-shaped invaginations that sense and respond to plasma membrane tension. However, the structural basis for caveolin's membrane remodeling activity is currently unknown. Here, we show that, using cryo-electron microscopy, the human caveolin-1 complex is composed of 11 protomers organized into a tightly packed disc with a flat membrane-embedded surface. The structural insights suggest a previously unrecognized mechanism for how membrane-sculpting proteins interact with membranes and reveal how key regions of caveolin-1, including its scaffolding, oligomerization, and intramembrane domains, contribute to its function.
External linksSci Adv / PubMed:35544577 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

25007

7sc0

EMDB-25007, PDB-7sc0:
CryoEM structure of the Caveolin-1 8S complex
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / caveolin / caveolae / cryoEM / disc / monotopic proteins

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