PRR11 induces filopodia formation and promotes cell motility via recruiting ARP2/3 complex in non-small cell lung cancer cells
| Autor: | Ying Zhang, Xun Yin, Yunlong Lei, Guoxiang Jin, Youquan Bu, Zhili Wei, Chundong Zhang, Jiaqian Wu, Yi Li, Ru Wang, lian Zhang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: |
Medicine (General)
Cell Arp2/3 complex Motility Integrin macromolecular substances Cell motility QH426-470 Biochemistry Chromatin remodeling Focal adhesion 03 medical and health sciences 0302 clinical medicine R5-920 Full Length Article medicine Genetics Molecular Biology Genetics (clinical) Actin 030304 developmental biology Filopodia 0303 health sciences biology ARP2/3 complex FAK Chemistry Cell Biology NSCLC cells Cell biology medicine.anatomical_structure 030220 oncology & carcinogenesis biology.protein PRR11 Lamellipodium |
| Zdroj: | Genes and Diseases, Vol 9, Iss 1, Pp 230-244 (2022) Genes & Diseases |
| ISSN: | 2352-3042 |
| Popis: | Filopodia, a finger-like structure and actin-rich plasma-membrane protrusion at the leading edge of the cell, has important roles in cell motility. However, the mechanisms of filopodia generation are not well-understood via the actin-related protein 2/3 (ARP2/3) complex in Non-Small Cell Lung Cancer (NSCLC) cells. We previously have demonstrated that PRR11 associates with the ARP2/3 complex to regulate cytoskeleton-nucleoskeleton assembly and chromatin remodeling. In this study, we further demonstrate that PRR11 involves in filopodia formation, focal adhesion turnover and cell motility through ARP2/3 complex. Cell phenotype assays revealed that the silencing of PRR11 increased cellular size and inhibited cell motility in NSCLC cells. Mechanistically, PRR11 recruited and co-localized with Arp2 at the membrane protrusion to promote filopodia formation but not lamellipodia formation. Notably, PRR11 mutant deletion of the proline-rich region 2 (amino acid residues 185–200) abrogated the effect of filopodia formation. In addition, PRR11-depletion inhibited filopodial actin filaments assembly and increased the level of active integrin β1 in the cell surface, whereas reduced the phosphorylation level of focal adhesion kinase (FAKY397) to repress focal adhesion turnover and cell motility in NSCLC cells. Taken together, our findings indicate that PRR11 has critical roles in controlling filopodia formation, focal adhesion turnover and cell motility by recruiting ARP2/3 complex, thus dysregualted expression of PRR11 potentially facilitates tumor metastasis in NSCLC cells. |
| Databáze: | OpenAIRE |
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