Dissecting the Structural Dynamics of the Nuclear Pore Complex.
Mol Cell
; 81(1): 153-165.e7, 2021 01 07.
Article
em En
| MEDLINE
| ID: mdl-33333016
ABSTRACT
Cellular processes are largely carried out by macromolecular assemblies, most of which are dynamic, having components that are in constant flux. One such assembly is the nuclear pore complex (NPC), an â¼50 MDa assembly comprised of â¼30 different proteins called Nups that mediates selective macromolecular transport between the nucleus and cytoplasm. We developed a proteomics method to provide a comprehensive picture of the yeast NPC component dynamics. We discovered that, although all Nups display uniformly slow turnover, their exchange rates vary considerably. Surprisingly, this exchange rate was relatively unrelated to each Nup's position, accessibility, or role in transport but correlated with its structural role; scaffold-forming Nups exchange slowly, whereas flexible connector Nups threading throughout the NPC architecture exchange more rapidly. Targeted perturbations in the NPC structure revealed a dynamic resilience to damage. Our approach opens a new window into macromolecular assembly dynamics.
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Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Schizosaccharomyces
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Poro Nuclear
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Complexo de Proteínas Formadoras de Poros Nucleares
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Proteínas de Saccharomyces cerevisiae
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Proteínas de Schizosaccharomyces pombe
Idioma:
En
Revista:
Mol Cell
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2021
Tipo de documento:
Article
País de afiliação:
Estados Unidos