Identification, sequence and developmental expression of invertebrate flotillins from Drosophila melanogaster

Galbiati, Ferruccio; Volonté, Daniela; Goltz, Jason S.; Steele, Zac; Sen, Jonaki; Jurcsak, Jennifer; Stein, David; Stevens, Leslie M.; Lisanti, Michael P.

doi:10.1016/s0378-1119(98)00064-x

Cited by 58 publications

(62 citation statements)

References 44 publications

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“…3), suggesting that we had successfully isolated caveolin-rich membranes. Large amounts of the protein flotillin-1 are also found in caveolae/lipid rafts (32). To further verify the isolation of caveola-related membranes, we probed for flotillin-1 and were able to observe the expected enrichment in fraction 2 (Fig.…”

Section: Accumulation Of Tritium In the Caveolin-rich Membrane Fractimentioning

confidence: 90%

A Role for Caveolae/Lipid Rafts in the Uptake and Recycling of the Endogenous Cannabinoid Anandamide

McFarland

Porter

Rakhshan

et al. 2004

Journal of Biological Chemistry

124

146

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The mechanisms responsible for the uptake and cellular processing of the endogenous cannabinoid anandamide are not well understood. We propose that anandamide uptake may occur via a caveola/lipid raft-related endocytic process in RBL-2H3 cells. Inhibitors of caveola-related (clathrin-independent) endocytosis reduced anandamide transport by ϳ50% compared with the control. Fluorescein derived from fluorescently labeled anandamide colocalized with protein markers of caveolae at early time points following transport. In this study, we have also identified a yet unrecognized process involved in trafficking events affecting anandamide following its uptake. Following uptake of [ 3 H]anandamide by RBL-2H3 cells, we found an accumulation of tritium in the caveolin-rich membranes. Inhibitors of both anandamide uptake and metabolism blocked the observed enrichment of tritium in the caveolin-rich membranes. Mass spectrometry of subcellular membrane fractions revealed that the tritium accumulation observed in the caveolin-rich membrane fraction was not representative of intact anandamide, suggesting that following metabolism by the enzyme fatty acid amide hydrolase (FAAH), anandamide metabolites are rapidly enriched in caveolae. Furthermore, HeLa cells, which do not express high levels of FAAH, showed an accumulation of tritium in the caveolin-rich membrane fraction only when transfected with FAAH cDNA. Western blot and immunocytochemistry analyses of RBL-2H3 cells revealed that FAAH was localized in intracellular compartments distinct from caveolin-1 localization. Together, these data suggest that following uptake via caveola/lipid raft-related endocytosis, anandamide is rapidly metabolized by FAAH, with the metabolites efficiently recycled to caveolin-rich membrane domains.

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Section: Accumulation Of Tritium In the Caveolin-rich Membrane Fractimentioning

confidence: 90%

A Role for Caveolae/Lipid Rafts in the Uptake and Recycling of the Endogenous Cannabinoid Anandamide

McFarland

Porter

Rakhshan

et al. 2004

Journal of Biological Chemistry

124

146

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“…Flotillins are integral membrane proteins that are enriched in lipid rafts, which also contain caveolins and glycosylphosphatidylinositol (GPI) -anchored proteins (Bickel et al, 1997;Galbiati et al, 1998;Lang et al, 1998). Lipid rafts are segregated cell membrane domains that are thought to be very important in a variety of signal transduction events (Bickel, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…Indeed, there is a paucity of descriptions of Flotillin expression patterns during development. In the initial description of Drosophila flotillin-1, wholemount staining was performed only during germ-band shortening (stages 12-16) to demonstrate transcripts in the brain and ventral nerve cord (Galbiati et al, 1998). In an initial characterization of an antibody directed against Flotillin (called Neurolin), immunostaining was performed only in day 5 goldfish larvae to demonstrate staining on retinal ganglion cells and their axons (Paschke et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Xenopus flotillin1, a novel gene highly expressed in the dorsal nervous system

Pandur

Dirksen

Moore

et al. 2004

Developmental Dynamics

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The two paralogues of the Xenopus flotillin1 gene (flotillin1A and flotillin1B), which encodes a putative membraneassociated protein, were cloned from egg, cleavage, and tadpole cDNA libraries. Both mRNAs are present during oogenesis and cleavage stages. After the onset of zygotic transcription, flotillin1 transcripts are first expressed throughout the embryonic ectoderm and become enhanced in the presumptive neural ectoderm as the neural plate forms. As the neural tube forms and differentiates, flotillin1 transcripts become enriched in the dorsal half, with particularly high expression in dorsal primary neurons. At early tail bud stages, there is additional expression in the paraxial mesoderm. At late tail bud stages, flotillin1A is expressed in branchial arch mesenchyme, the overlying branchial ectoderm and in dorsal somitic mesoderm, whereas flotillin1B expression is more restricted in the dorsal neural tube and head sensory structures. This report is the first comprehensive developmental description in any animal of the expression pattern of this gene, whose protein product in several systems plays important roles in signal transduction events. Developmental Dynamics 231:881-887, 2004.

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“…The independent identification of mice and fruitfly homologues led to the alternative names flotillin-1 and -2 (reggie-2 and -1, respectively) [4,5]. Although they were initially thought to be components of caveolae [4], subsequent biochemical and microscopic characterization revealed that these 48-kDa proteins are distinctive non-caveolar markers of detergent-resistant microdomains (DRMs) [3,6].…”

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confidence: 99%

“…Reggies/flotillins do not have typical transmembrane domains, but harbor two conserved hydrophobic stretches that allow potential interactions with the inner leaflet of the plasma membrane, and possibly protein-protein interactions [7,8]. Notably, reggies/flotillins are expressed in most cell types [3,6], including those devoid of caveolae, such as neurons [3,5], and lymphocytes [6,[10][11][12]. Their subcellular distribution under light microscopy (LM) typically consists of a punctate membrane co-localization pattern [3], indicative of small (≤0.1 mm) microdomains, as revealed by electron microscopy (EM) studies [6].…”

mentioning

confidence: 99%

Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: convergent evolution of the SPFH domain

Rivera-Milla

Stuermer

Málaga-Trillo

2006

Cell. Mol. Life Sci.

147

150

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Abstract. Reggies (flotillins) are detergent-resistant microdomains involved in the scaffolding of large heteromeric complexes that signal across the plasma membrane. Based on the presence of an evolutionarily widespread motif, reggies/flotillins have been included within the SPFH (stomatin-prohibitin-flotillin-HflC/K) protein superfamily. To better understand the origin and evolution of reggie/flotillin structure and function, we searched databases for reggie/flotillin and SPFH-like proteins in organisms at the base and beyond the animal kingdom, and used the resulting dataset to compare their structural Cell. Mol. Life Sci. 63 (2006) 343-357 1420-682X/06/030343-15 DOI 10.1007/s00018-005-5434-3 © Birkhäuser Verlag, Basel, 2006 and functional domains. Our analysis shows that the SPFH grouping has little phylogenetic support, probably due to convergent evolution of its members. We also find that reggie/flotillin homologues are highly conserved among metazoans but are absent in plants, fungi and bacteria, where only proteins with 'reggie-like' domains can be found. However, despite their low sequence similarities, reggie/flotillin and 'reggie-like' domains appear to subserve related functions, suggesting that their basic biological role was acquired independently during evolution.

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Identification, sequence and developmental expression of invertebrate flotillins from Drosophila melanogaster

Cited by 58 publications

References 44 publications

A Role for Caveolae/Lipid Rafts in the Uptake and Recycling of the Endogenous Cannabinoid Anandamide

A Role for Caveolae/Lipid Rafts in the Uptake and Recycling of the Endogenous Cannabinoid Anandamide

Xenopus flotillin1, a novel gene highly expressed in the dorsal nervous system

Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: convergent evolution of the SPFH domain

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