Flotillin and Epidermal Surface Antigen Define a New Family of Caveolae-associated Integral Membrane Proteins

Bickel, Perry E.; Scherer, Philipp E.; Schnitzer, Jan E.; Oh, Phil; Lisanti, Michael P.; Lodish, Harvey F.

doi:10.1074/jbc.272.21.13793

Cited by 528 publications

(569 citation statements)

References 42 publications

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“…The pattern of palmitoylation is rather variable, with two experimentally confirmed palmitoylated sites in reggie-1 (human Cys-4 and Cys-38), and three sites in reggie-2 (human Cys-5, Cys-17 and Cys-34) [7,8]. Four putative phosphorylation sites are conserved in all reggies/flotillins examined [3,4], with some differences in their location in Ciona reggie-1 ( fig. 1).…”

Section: Resultsmentioning

confidence: 99%

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confidence: 99%

“…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]. In humans, reggie-1 and reggie-2 polypeptides show similar length, primary sequence composition and biochemical profiles, with a conserved protein architecture at the N terminus containing one myristoylation site (Gly-2, only in reggie-1) and four palmitoylation sites (Cys-5, Cys-19, Cys-20, Cys-38), which are thought to assist in membrane association and lipid raft targeting [7][8][9].…”

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confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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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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“…Despite the absence of caveolin, DIGs can be isolated from neuronal sources and are found to contain a number of GPI-anchored proteins, such as alkaline phosphatase, 5h-nucleotidase, F3 protein, the prion protein [24][25][26][27], tyrosine kinases, and α-and β-subunits of heterotrimeric G-proteins [28,29]. Another protein, flotillin, has been found to be present exclusively in DIGs isolated from neuronal sources and can, therefore, be used in place of caveolin as a transmembrane polypeptide-anchored marker for these membrane domains [30][31][32].…”

Section: Introductionmentioning

confidence: 99%

Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein

Parkin

Turner

Hooper

1999

Biochemical Journal

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Lipid rafts are regions of the plasma membrane that are enriched in cholesterol, glycosphingolipids and acylated proteins, and which have been proposed as sites for the proteolytic processing of the Alzheimer's amyloid precursor protein (APP). Lipid rafts can be isolated on the basis of their insolubility in Triton X-100 at 4 mC, with the resulting low-density, detergent-insoluble glycolipid-enriched fraction (DIG) being isolated by flotation through a sucrose density gradient. The detergent-insolubility of APP in mouse cerebral cortex relative to a variety of DIG marker proteins (alkaline phosphatase, flotillin, F3 protein and prion protein) and non-DIG proteins (alkaline phosphodiesterase I, aminopeptidase A and clathrin) has been examined. Alkaline phosphatase, flotillin, F3 protein and the prion protein were present exclusively in the DIG region of the sucrose gradient over a range of protein\detergent ratios used to solubilize the membranes and displayed a characteristic enrichment in the lowdensity fraction as the protein\detergent ratio was decreased. In

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“…Flotillin-1 (FLOT1), also known as Reggie-2, encodes a caveolae-associated, integral membrane protein [58]. Caveolae are small indentations on the plasma membrane that are involved in vesicular trafficking and signal transduction.…”

Section: Discussionmentioning

confidence: 99%

Identification of genes differentially expressed in T cells following stimulation with the chemokines CXCL12 and CXCL10

Smith

Shaw

et al. 2004

BMC Immunol

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BackgroundChemokines are involved in many biological activities ranging from leukocyte differentiation to neuronal morphogenesis. Despite numerous reports describing chemokine function, little is known about the molecular changes induced by cytokines.MethodsWe have isolated and identified by differential display analysis 182 differentially expressed cDNAs from CXCR3-transfected Jurkat T cells following treatment with CXCL12 or CXCL10. These chemokine-modulated genes were further verified using quantitative RT-PCR and Western blot analysis.ResultsOne hundred and forty-six of the cDNAs were successfully cloned, sequenced, and identified by BLAST. Following removal of redundant and non-informative clones, seventeen mRNAs were found to be differentially expressed post treatment with either chemokine ligand with several representing known genes with established functions. Twenty-one genes were upregulated in these transfected Jurkat cells following both CXCL12 and CXCL10, four genes displayed a discordant response and seven genes were downregulated upon treatment with either chemokine. Identified genes include geminin (GEM), thioredoxin (TXN), DEAD/H box polypeptide 1 (DDX1), growth hormone inducible transmembrane protein (GHITM), and transcription elongation regulator 1 (TCERG1). Subsequent analysis of several of these genes using semi-quantitative PCR and western blot analysis confirmed their differential expression post ligand treatment.ConclusionsTogether, these results provide insight into chemokine-induced gene activation and identify potentially novel functions for known genes in chemokine biology.

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Flotillin and Epidermal Surface Antigen Define a New Family of Caveolae-associated Integral Membrane Proteins

Cited by 528 publications

References 42 publications

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

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

Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein

Identification of genes differentially expressed in T cells following stimulation with the chemokines CXCL12 and CXCL10

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