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-Structure paper
タイトル | Molecular architecture of the human caveolin-1 complex. |
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ジャーナル・号・ページ | Sci Adv, Vol. 8, Issue 19, Page eabn7232, Year 2022 |
掲載日 | 2022年5月13日 |
![]() | Jason 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 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.4 Å |
構造データ | EMDB-25007, PDB-7sc0: |
由来 |
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![]() | STRUCTURAL PROTEIN / caveolin / caveolae / cryoEM / disc / monotopic proteins |