A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane
Open Access
- 4 September 2007
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 178 (6), 897-904
- https://doi.org/10.1083/jcb.200702026
Abstract
The type II inner nuclear membrane protein emerin is a component of the LINC complex that connects the nuclear lamina to the actin cytoskeleton. In emerin-null or -deficient human dermal fibroblasts we find that the centrosome is detached from the nucleus. Moreover, following siRNA knockdown of emerin in wild-type fibroblasts, the centrosome also becomes detached from the nucleus. We show that emerin interacts with tubulin, and that nocadozole-treated wild-type cells phenocopy the detached centrosome characteristic of emerin-null/deficient cells. We also find that a significant fraction of emerin is located at the outer nuclear membrane and peripheral ER, where it interacts directly with the centrosome. Our data provide the first evidence in mammalian cells as to the nature of the linkage of the centrosome, and therefore the tubulin cytoskeleton, with the outer nuclear membrane.Keywords
This publication has 29 references indexed in Scilit:
- Distinct functional domains in nesprin-1α and nesprin-2β bind directly to emerin and both interactions are disrupted in X-linked Emery–Dreifuss muscular dystrophyExperimental Cell Research, 2007
- The inner nuclear membrane protein Emerin regulates β-catenin activity by restricting its accumulation in the nucleusThe EMBO Journal, 2006
- Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectinThe Journal of cell biology, 2005
- Lamin A/C–dependent Localization of Nesprin-2, a Giant Scaffolder at the Nuclear EnvelopeMolecular Biology of the Cell, 2005
- Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscleJournal of Cell Science, 2005
- Lamins: building blocks or regulators of gene expression?Nature Reviews Molecular Cell Biology, 2002
- Nesprin‐1α self‐associates and binds directly to emerin and lamin A in vitroFEBS Letters, 2002
- Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger–Huët anomaly)Nature Genetics, 2002
- Colocalization of Emerin and Lamins in Interphase Nuclei and Changes during MitosisBiochemical and Biophysical Research Communications, 1998
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970