Publikation: Membrane and raft association of reggie-1/flotillin-2 : role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression
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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, phagocytosis 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.
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NEUMANN-GIESEN, Carolin, Bianca FALKENBACH, Peter BEICHT, Stephanie CLAASEN, Georg LÜERS, Claudia STÜRMER, Volker HERZOG, Ritva TIKKANEN, 2004. Membrane and raft association of reggie-1/flotillin-2 : role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression. In: Biochemical Journal. 2004, 378(2), pp. 509-518. ISSN 0264-6021. eISSN 1470-8728. Available under: doi: 10.1042/bj20031100BibTex
@article{NeumannGiesen2004Membr-8611,
year={2004},
doi={10.1042/bj20031100},
title={Membrane and raft association of reggie-1/flotillin-2 : role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression},
number={2},
volume={378},
issn={0264-6021},
journal={Biochemical Journal},
pages={509--518},
author={Neumann-Giesen, Carolin and Falkenbach, Bianca and Beicht, Peter and Claasen, Stephanie and Lüers, Georg and Stürmer, Claudia and Herzog, Volker and Tikkanen, Ritva}
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<dcterms:abstract xml:lang="eng">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, phagocytosis 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.</dcterms:abstract>
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