Topic
Spectrin repeat
About: Spectrin repeat is a research topic. Over the lifetime, 108 publications have been published within this topic receiving 6911 citations. The topic is also known as: Spectrin_repeat & IPR002017.
Papers published on a yearly basis
Papers
TL;DR: Plectin binds to the integrin α6β4 at the cell surface and to nesprin-3 at the ONM in keratinocytes, suggesting that there is a continuous connection between the nucleus and the extracellular matrix through the IF cytoskeleton.
Abstract: Despite their importance in cell biology, the mechanisms that maintain the nucleus in its proper position in the cell are not well understood. This is primarily the result of an incomplete knowledge of the proteins in the outer nuclear membrane (ONM) that are able to associate with the different cytoskeletal systems. Two related ONM proteins, nuclear envelope spectrin repeat (nesprin)–1 and –2, are known to make direct connections with the actin cytoskeleton through their NH2-terminal actin-binding domain (ABD). We have now isolated a third member of the nesprin family that lacks an ABD and instead binds to the plakin family member plectin, which can associate with the intermediate filament (IF) system. Overexpression of nesprin-3 results in a dramatic recruitment of plectin to the nuclear perimeter, which is where these two molecules are colocalized with both keratin-6 and -14. Importantly, plectin binds to the integrin α6β4 at the cell surface and to nesprin-3 at the ONM in keratinocytes, suggesting that there is a continuous connection between the nucleus and the extracellular matrix through the IF cytoskeleton.
495 citations
TL;DR: The α-actinin rod domain this paper forms a rigid connection between two actin-binding domains positioned at the two ends of the dimer, which is important for organizing muscle Z-line and maintaining its architecture during muscle contraction.
307 citations
TL;DR: It is proposed that membrane‐anchored nesprin‐1α antiparallel dimers interact with both emerin and lamin A to provide scaffolding at the inner nuclear membrane.
263 citations
TL;DR: The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod.
252 citations
TL;DR: Recent advances in the understanding of how nesprins couple to various filamentous systems within the cell are reviewed and the importance of both KASH and KASH-less nesPRin isoforms in these interactions are emphasised.
172 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 4 |
| 2020 | 7 |
| 2019 | 3 |
| 2018 | 2 |
| 2017 | 1 |
| 2016 | 6 |