Dissecting the molecular function of reggie/flotillin proteins

Babuke, Tanja; Tikkanen, Ritva

doi:10.1016/j.ejcb.2007.03.003

Cited by 153 publications

(126 citation statements)

References 49 publications

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“…Conversely, Reggie-1 overexpression inhibits short-range and activates long-range targets, even when Reggie-1 expression is restricted to Wgexpressing cells. As Reggie-1 is implicated in vesicular trafficking (Babuke and Tikkanen 2007;Langhorst et al 2008) and Wg can associate with lipid rafts (Zhai et al 2004), these data suggest Reggie-1 works with Dly to promote Wg transcytosis and subsequent long-range diffusion (Fig. 2).…”

Section: Getting Out and About-wnt Secretion And Transportmentioning

confidence: 90%

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Wnt Signaling from Development to Disease: Insights from Model Systems

Cadigan¹,

Peifer²

2009

Cold Spring Harbor Perspectives in Biology

277

259

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One of the early surprises in the study of cell adhesion was the discovery that b-catenin plays dual roles, serving as an essential component of cadherin-based cell -cell adherens junctions and also serving as the key regulated effector of the Wnt signaling pathway. Here, we review our current model of Wnt signaling and discuss how recent work using model organisms has advanced our understanding of the roles Wnt signaling plays in both normal development and in disease. These data help flesh out the mechanisms of signaling from the membrane to the nucleus, revealing new protein players and providing novel information about known components of the pathway.

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Section: Getting Out and About-wnt Secretion And Transportmentioning

confidence: 90%

“…Reggie-1 (Flotillin-2) is a cytoplasmic component of noncaveolin lipid microdomains (Babuke and Tikkanen 2007;Langhorst et al 2005). Reggie-1 loss strongly reduces longrange Wg targets but has no effect on shortrange targets (Katanaev et al 2008).…”

Section: Getting Out and About-wnt Secretion And Transportmentioning

confidence: 99%

Wnt Signaling from Development to Disease: Insights from Model Systems

Cadigan¹,

Peifer²

2009

Cold Spring Harbor Perspectives in Biology

277

259

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“…Flotillins are lipid raft scaffold proteins and have been reported to be involved in a variety of cellular processes (8)(9)(10)(11). However, their role in cholesterol absorption in mammals has not been studied.…”

Section: Discussionmentioning

confidence: 99%

“…Here, we unravel an important role of flotillin-1 and flotillin-2, two homologous lipid raft proteins belonging to stomatin-prohibitin-flotillin-HflK/C (SPFH) domain family (8)(9)(10)(11), in NPC1L1-mediated cellular cholesterol uptake and biliary cholesterol reabsorption.…”

mentioning

confidence: 99%

Flotillins play an essential role in Niemann-Pick C1-like 1-mediated cholesterol uptake

Qi²,

Wang³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

145

140

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Dietary absorption is a major way for mammals to obtain cholesterol, which is mediated by Niemann-Pick C1-like 1 (NPC1L1) via vesicular endocytosis. One fundamental question in this process is how free cholesterol is efficiently taken up through the internalization of NPC1L1. Using exogenously expressed NPC1L1-EGFP, we show that the lipid raft proteins flotillins associate with NPC1L1 and their localization is regulated by NPC1L1 during intracellular trafficking. Furthermore, flotillins are essential for NPC1L1-mediated cellular cholesterol uptake, biliary cholesterol reabsorption, and the regulation of lipid levels in mice. Together with NPC1L1, they form cholesterol-enriched membrane microdomains, which function as carriers for bulk of cholesterol. The hypocholesterolemic drug ezetimibe disrupts the association between NPC1L1 and flotillins, which blocks the formation of the cholesterol-enriched microdomains. Our findings reveal a functional role of flotillins in NPC1L1-mediated cholesterol uptake and elucidate the formation of NPC1L1-flotillins-postive cholesterol-enriched membrane microdomains as a mechanism for efficient cholesterol absorption.

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“…Interestingly, it has been shown that flotillin-1 and flotillin-2 (also known as reggie-2 and -1) are localised in lipid rafts [37] and co-localise with GPI-anchored cell adhesion molecules, known to be found in rafts. It is necessary to note here that, although the outer leaflet of lipid rafts (Fig.…”

Section: Lipid Raftsmentioning

confidence: 99%

Lipid Rafts and Caveolae in Signaling by Growth Factor Receptors

Laurentiis¹,

Donovan²,

Arcaro³

2007

TOBIOCJ

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Lipid rafts and caveolae are microdomains of the plasma membrane enriched in sphingolipids and cholesterol, and hence are less fluid than the remainder of the membrane. Caveolae have an invaginated structure, while lipid rafts are flat regions of the membrane. The two types of microdomains have different protein compositions (growth factor receptors and their downstream molecules) suggesting that lipid rafts and caveolae have a role in the regulation of signaling by these receptors. The purpose of this review is to discuss this model, and the implications that it might have regarding a potential role for lipid rafts and caveolae in human cancer. Particular attention will be paid to the epidermal growth factor receptor, for which the largest amount of information is available. It has been proposed that caveolins act as tumor suppressors. The role of lipid rafts is less clear, but they seem to be capable of acting as 'signaling platforms', in which signal initiation and propagation can occur efficiently.

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Dissecting the molecular function of reggie/flotillin proteins

Cited by 153 publications

References 49 publications

Wnt Signaling from Development to Disease: Insights from Model Systems

Wnt Signaling from Development to Disease: Insights from Model Systems

Flotillins play an essential role in Niemann-Pick C1-like 1-mediated cholesterol uptake

Lipid Rafts and Caveolae in Signaling by Growth Factor Receptors

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