Journalartikel
Autorenliste: Neumann-Giesen, Carolin; Falkenbach, Bianca; Beicht, Peter; Claasen, Stephanie; Lüers, Georg; Stuermer, Claudia AO; Herzog, Volker; Tikkanen, Ritva
Jahr der Veröffentlichung: 2004
Seiten: 509-518
Zeitschrift: Biochemical Journal
Bandnummer: 378
ISSN: 0264-6021
eISSN: 1470-8728
DOI Link: https://doi.org/10.1042/BJ20031100
Verlag: Portland Press
Abstract:
The reggie protein family consists of two proteins, reggie-1 and -2, also called flotillins, which are highly ubiquitous and evolutionarily conserved. Both reggies have been shown to be associated with membrane rafts and are involved in various cellular processes such as T-cell activation, phargocytosis and insulin signalling. However, the exact molecular function of these proteins remains to be determined. In addition, the mechanism of membrane association of reggie-1, which does not contain any transmembrane domain, is not known. In this study, we have produced a fusion protein of reggie-1 with enhanced green fluorescent protein and generated targeted substitutions for the inactivation of putative palmitoylation and myristoylation sites. We were able to show that reggie-1 is myristoylated and multiply palmitoylated and that lipid modifications are necessary for membrane association of reggie-1. Overexpression of reggie-1 resulted in the induction of numerous filopodia-like protrusions in various cell lines, suggesting a role for reggie-1 as a signalling protein in actin-dependent processes.
Zitierstile
Harvard-Zitierstil: Neumann-Giesen, C., Falkenbach, B., Beicht, P., Claasen, S., Lüers, G., Stuermer, C., et al. (2004) Membrane and raft association of reggie-1/flotillin-2:: role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression, Biochemical Journal, 378, pp. 509-518. https://doi.org/10.1042/BJ20031100
APA-Zitierstil: Neumann-Giesen, C., Falkenbach, B., Beicht, P., Claasen, S., Lüers, G., Stuermer, C., Herzog, V., & Tikkanen, R. (2004). Membrane and raft association of reggie-1/flotillin-2:: role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression. Biochemical Journal. 378, 509-518. https://doi.org/10.1042/BJ20031100
