Journal article

Publication year: 2011

Pages: 725-735

Journal: Current Protein & Peptide Science

Volume number: 12

Issue number: 8

ISSN: 1389-2037

eISSN: 1875-5550

DOI Link: https://doi.org/10.2174/138920311798841708

Publisher: Bentham Science Publishers

Abstract: 
Flotillin-2 and flotillin-1, also called reggie-1 and reggie-2, are ubiquitously expressed and highly conserved proteins. Originally, they were described as neuronal regeneration proteins, but they appear to function in a wide variety of cellular processes, such as membrane receptor signaling, endocytosis, phagocytosis and cell adhesion. The molecular details of the function of flotillins in these processes have only been partially clarified. Flotillins are associated with cholesterol and sphingolipid enriched membrane microdomains known as rafts, and some findings even suggest that they define their own kind of a microdomain. The mechanism of the membrane association of flotillins appears to rely mainly on acylation (myristoylation and/or palmitoylation), localizing flotillins onto the cytosolic side of the membranes, whereas no transmembrane domains are present. In addition, flotillins show a strong tendency to form homo-and hetero-oligomers with each other. In this review, we will summarize the recent findings on the function of flotillins and discuss the mechanisms that might regulate their function, such as membrane association, oligomerization and phosphorylation.

Harvard Citation style: Banning, A., Tomasovic, A. and Tikkanen, R. (2011) Functional Aspects of Membrane Association of Reggie/Flotillin Proteins, Current Protein & Peptide Science, 12(8), pp. 725-735. https://doi.org/10.2174/138920311798841708

APA Citation style: Banning, A., Tomasovic, A., & Tikkanen, R. (2011). Functional Aspects of Membrane Association of Reggie/Flotillin Proteins. Current Protein & Peptide Science. 12(8), 725-735. https://doi.org/10.2174/138920311798841708