Symmetry disruption commits vault particles to disassembly
EntityUAM. Departamento de Física de la Materia Condensada
PublisherAmerican Association for the Advancement of Science
10.1126/sciadv.abj7795Science Advances 8.6 (2022): eabj7795
SubjectsCellular Process; Inner Cavities; Major Vault Proteins; Ribonucleoprotein Particles; Nano-Devices; Física
Rights© 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science
Esta obra está bajo una Licencia Creative Commons Atribución 4.0 Internacional.
Vaults are ubiquitous ribonucleoprotein particles involved in a diversity of cellular processes, with promising applications as nanodevices for delivery of multiple cargos. The vault shell is assembled by the symmetrical association of multiple copies of the major vault protein that, initially, generates half vaults. The pairwise, anti-parallel association of two half vaults produces whole vaults. Here, using a combination of vault recombinant reconstitution and structural techniques, we characterized the molecular determinants for the vault opening process. This process commences with a relaxation of the vault waist, causing the expansion of the inner cavity. Then, local disengagement of amino-terminal domains at the vault midsection seeds a conformational change that leads to the aperture, facilitating access to the inner cavity where cargo is hosted. These results inform a hitherto uncharacterized step of the vault cycle and will aid current engineering efforts leveraging vault for tailored cargo delivery
Google Scholar:Guerra, Pablo - González-Alamos, María - Llauró Portell, Aida - Casañas, Arnau - Querol-Audí, Jordi - Pablo Gómez, Pedro José de - Verdaguer, Núria
This item appears in the following Collection(s)
Showing items related by title, author, creator and subject.