期刊
DEVELOPMENTAL CELL
卷 38, 期 4, 页码 371-383出版社
CELL PRESS
DOI: 10.1016/j.devcel.2016.07.021
关键词
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资金
- Medical Research Council (MRC) [MR/J000647/1]
- Royal Society
- Wellcome Trust [WT092825]
- MRC [MR/J000647/1, MC_PC_14105, MR/K015664/1] Funding Source: UKRI
- Medical Research Council [MC_PC_14105, MR/K015664/1, MR/J000647/1] Funding Source: researchfish
Fascin is an F-actin-bundling protein shown to stabilize filopodia and regulate adhesion dynamics in migrating cells, and its expression is correlated with poor prognosis and increased metastatic potential in a number of cancers. Here, we identified the nuclear envelope protein nesprin-2 as a binding partner for fascin in a range of cell types in vitro and in vivo. Nesprin-2 interacts with fascin through a direct, F-actin-independent interaction, and this binding is distinct and separable from a role for fascin within filopodia at the cell periphery. Moreover, disrupting the interaction between fascin and nesprin-2 C-terminal domain leads to specific defects in F-actin coupling to the nuclear envelope, nuclear movement, and the ability of cells to deform their nucleus to invade through confined spaces. Together, our results uncover a role for fascin that operates independently of filopodia assembly to promote efficient cell migration and invasion.
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