| Range |
microtubules 24: filamentous actin 8: vimentin 10: lamin meshwork ~3.5 nm
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| Organism |
Unspecified |
| Reference |
Turgay Y et al., (2017). The molecular architecture of lamins in somatic cells. Nature. 2017 Mar 9 543(7644):261-264. doi: 10.1038/nature21382 p.263 figure 4b & p.264 left column 2nd paragraphPubMed ID28241138
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| Primary Source |
[25] Nogales, E., Wolf, S. G., Khan, I. A., Ludueña, R. F. & Downing, K. H. Structure of tubulin at 6.5 A and location of the taxol-binding site. Nature 375, 424–427 (1995) DOI: 10.1038/375424a0 [26] Galkin, V. E., Orlova, A., Vos, M. R., Schröder, G. F. & Egelman, E. H. Near-atomic resolution for one state of F-actin. Structure 23, 173–182 (2015) DOI: 10.1016/j.str.2014.11.006PubMed ID7760939, 25533486
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| Method |
Abstract: "Here [investigators] 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 3.5nm thickness." |
| Comments |
P.264 left column 2nd paragraph: "On the basis of their genealogy, lamins are considered to be the evolutionary ancestors of all cytoskeletal intermediate filaments [ref 24]. However, it is apparent that lamins form a different filamentous structure compared with cytoplasmic intermediate filament proteins. Figure 4b shows the major cytoskeletal elements for comparison with the nuclear lamins. Microtubules exhibit a 24 nm thick tubular structure [primary source 25], filamentous actin assembles into an 8 nm thick helical structure [primary source 26], and cytoplasmic intermediate filaments, for example vimentin, into 10 nm thick filaments. Here [investigators] show that the lamin meshwork is composed of ∼3.5 nm thick filaments, which distinguishes them from the other cytoskeletal constituents in higher eukaryotes." |
| Entered by |
Uri M |
| ID |
114288 |