Other
15 Authors
- Nmezi B,
- Stolz DB,
- Xu J,
- Fu R,
- Chen NY,
- Padiath QS,
- Liu Y,
- Armiger TJ,
- Young SG,
- Dahl KN,
- Sullivan M,
- Ma H,
- Tu Y,
- Powell JS,
- Rodriguez-Bey G
| First Author | Nmezi B | Year | 2019 |
| Journal | Proc Natl Acad Sci U S A | PubMed ID | 30765529 |
| Mgi Jnum | J:273913 | Mgi Id | MGI:6283206 |
| Doi | 10.1073/pnas.1810070116 | Citation | Nmezi B, et al. (2019) Concentric organization of A- and B-type lamins predicts their distinct roles in the spatial organization and stability of the nuclear lamina. Proc Natl Acad Sci U S A |
| abstractText | The nuclear lamina is an intermediate filament meshwork adjacent to the inner nuclear membrane (INM) that plays a critical role in maintaining nuclear shape and regulating gene expression through chromatin interactions. Studies have demonstrated that A- and B-type lamins, the filamentous proteins that make up the nuclear lamina, form independent but interacting networks. However, whether these lamin subtypes exhibit a distinct spatial organization or whether their organization has any functional consequences is unknown. Using stochastic optical reconstruction microscopy (STORM) our studies reveal that lamin B1 and lamin A/C form concentric but overlapping networks, with lamin B1 forming the outer concentric ring located adjacent to the INM. The more peripheral localization of lamin B1 is mediated by its carboxyl-terminal farnesyl group. Lamin B1 localization is also curvature- and strain-dependent, while the localization of lamin A/C is not. We also show that lamin B1's outer-facing localization stabilizes nuclear shape by restraining outward protrusions of the lamin A/C network. These two findings, that lamin B1 forms an outer concentric ring and that its localization is energy-dependent, are significant as they suggest a distinct model for the nuclear lamina-one that is able to predict its behavior and clarifies the distinct roles of individual nuclear lamin proteins and the consequences of their perturbation. |
