| Literature DB >> 28241138 |
Yagmur Turgay1, Matthias Eibauer1, Anne E Goldman2, Takeshi Shimi2, Maayan Khayat3, Kfir Ben-Harush4, Anna Dubrovsky-Gaupp1, K Tanuj Sapra1, Robert D Goldman2, Ohad Medalia1,3.
Abstract
The nuclear lamina is a fundamental constituent of metazoan nuclei. It is composed mainly of lamins, which are intermediate filament proteins that assemble into a filamentous meshwork, bridging the nuclear envelope and chromatin. Besides providing structural stability to the nucleus, the lamina is involved in many nuclear activities, including chromatin organization, transcription and replication. However, the structural organization of the nuclear lamina is poorly understood. Here we use cryo-electron tomography to obtain a detailed view of the organization of the lamin meshwork within the lamina. Data analysis of individual lamin filaments resolves a globular-decorated fibre appearance and shows that A- and B-type lamins assemble into tetrameric filaments of 3.5 nm thickness. Thus, lamins exhibit a structure that is remarkably different from the other canonical cytoskeletal elements. Our findings define the architecture of the nuclear lamin meshworks at molecular resolution, providing insights into their role in scaffolding the nuclear lamina.Entities:
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Year: 2017 PMID: 28241138 PMCID: PMC5616216 DOI: 10.1038/nature21382
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962