Journalartikel
Autorenliste: Banning, Antje; Babuke, Tanja; Kurrle, Nina; Meister, Melanie; Ruonala, Mika O.; Tikkanen, Ritva
Jahr der Veröffentlichung: 2018
Zeitschrift: Cells
Bandnummer: 7
Heftnummer: 4
eISSN: 2073-4409
Open Access Status: Gold
DOI Link: https://doi.org/10.3390/cells7040028
Verlag: MDPI
Abstract:
Cell-matrix adhesion and cell migration are physiologically important processes that also play a major role in cancer spreading. In cultured cells, matrix adhesion depends on integrin-containing contacts such as focal adhesions. Flotillin-1 and flotillin-2 are frequently overexpressed in cancers and are associated with poor survival. Our previous studies have revealed a role for flotillin-2 in cell-matrix adhesion and in the regulation of the actin cytoskeleton. We here show that flotillins are important for cell migration in a wound healing assay and influence the morphology and dynamics of focal adhesions. Furthermore, anchorage-independent growth in soft agar is enhanced by flotillins. In the absence of flotillins, especially flotillin-2, phosphorylation of focal adhesion kinase and extracellularly regulated kinase is diminished. Flotillins interact with alpha-actinin, a major regulator of focal adhesion dynamics. These findings are important for understanding the molecular mechanisms of how flotillin overexpression in cancers may affect cell migration and, especially, enhance metastasis formation.
Zitierstile
Harvard-Zitierstil: Banning, A., Babuke, T., Kurrle, N., Meister, M., Ruonala, M. and Tikkanen, R. (2018) Flotillins Regulate Focal Adhesions by Interacting with α-Actinin and by Influencing the Activation of Focal Adhesion Kinase, Cells, 7(4), Article 28. https://doi.org/10.3390/cells7040028
APA-Zitierstil: Banning, A., Babuke, T., Kurrle, N., Meister, M., Ruonala, M., & Tikkanen, R. (2018). Flotillins Regulate Focal Adhesions by Interacting with α-Actinin and by Influencing the Activation of Focal Adhesion Kinase. Cells. 7(4), Article 28. https://doi.org/10.3390/cells7040028
Schlagwörter
focal adhesion; INDUCED TYROSINE PHOSPHORYLATION; METASTASIS; MICRODOMAINS; REGGIE-1/FLOTILLIN-2; REGGIE/FLOTILLIN