A Polyaromatic Caveolin-Binding-Like Motif in the Cytoplasmic Tail of the Type 1 Receptor for Angiotensin II Plays an Important Role in Receptor Trafficking and Signaling

Leclerc, Patrice C.; Auger‐Messier, Mannix; Lanctot, Pascal M.; Escher, Emanuel; Leduc, Richard; Guillemette, Gaétan

doi:10.1210/en.2002-220679

Cited by 82 publications

(54 citation statements)

References 38 publications

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“…More recently, some groups have reported the association of the AT 1 with lipid rafts in different tissues [52][53][54]. Although the proper nature of this association is still debated, we can theorize that the identical subcellular localization of components of the insulin and Ang II signaling systems could provide yet another point of confluence between both pathways.…”

Section: The Cross-talk At the Extracellular Levelmentioning

confidence: 98%

The multi‐faceted cross‐talk between the insulin and angiotensin II signaling systems

Velloso

Folli

Perego

et al. 2006

Diabetes Metabolism Res

102

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SummaryInsulin and angiotensin II are hormones that play pivotal roles in the control of two vital and closely related systems, the metabolic and the circulatory systems, respectively. A failure in the proper action of each of these hormones results, to a variable degree, in the development of two highly prevalent and commonly overlapping diseases -diabetes mellitus and hypertension. In recent years, a series of studies has revealed a tight connection between the signal transduction pathways that mediate insulin and angiotensin II actions in target tissues. This molecular cross-talk occurs at multiple levels and plays an important role in phenomena that range from the action of anti-hypertensive drugs to cardiac hypertrophy and energy acquisition by the heart. At the extracellular level, the angiotensin-converting enzyme controls angiotensin II synthesis but also interferes with insulin signaling through the proper regulation of angiotensin II and through the accumulation of bradykinin. At an early intracellular level, angiotensin II, acting through JAK-2/IRS-1/PI3-kinase, JNK and ERK, may induce the serine phosphorylation and inhibition of key elements of the insulin-signaling pathway. Finally, by inducing the expression of the regulatory protein SOCS-3, angiotensin II may impose a late control on the insulin signal. This review will focus on the main advances obtained in this field and will discuss the implications of this molecular cross-talk in the common clinical association between diabetes mellitus and hypertension.

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Section: The Cross-talk At the Extracellular Levelmentioning

confidence: 98%

The multi‐faceted cross‐talk between the insulin and angiotensin II signaling systems

Velloso

Folli

Perego

et al. 2006

Diabetes Metabolism Res

102

View full text Add to dashboard Cite

show abstract

“…In this review, we will cover four major aspects of chemokine receptor trafficking: clathrin mediated endocytosis; caveolae/lipid raft mediated by intercalated cholesterol molecules [30][31][32]. Several GPCRs have been shown to signal in lipid rafts/caveolae [33][34][35][36]. At present, at least two chemokine receptors, CCR5 and CXCR4, have been identified to some degree in raft membranes [37][38][39].…”

Section: Introductionmentioning

confidence: 99%

Chemokine receptor internalization and intracellular trafficking

Neel

Schutyser

Sai

et al. 2005

Cytokine & Growth Factor Reviews

199

218

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The internalization and intracellular trafficking of chemokine receptors have important implications for the cellular responses elicited by chemokine receptors. The major pathway by which chemokine receptors internalize is the clathrin-mediated pathway, but some receptors may utilize lipid rafts/ caveolae-dependent internalization routes. This review discusses the current knowledge and controversies regarding these two different routes of endocytosis. The functional consequences of internalization and the regulation of chemokine receptor recycling will also be addressed. Modifications of chemokine receptors, such as palmitoylation, ubiquitination, glycosylation, and sulfation, may also impact trafficking, chemotaxis and signaling. Finally, this review will cover the internalization and trafficking of viral and decoy chemokine receptors.

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“…This binding site is found in the C-terminal part of PAFR, which also contains a potential binding motif for caveolin-1, a motif shared by many caveolin-binding proteins, such as G proteins and endothelial NOS. This motif was also found to be present in the AT1 receptor, but apparently was not important for AT1 location in caveolae (44). Our data, however, suggest that this PAFR motif is important not only for PAFR association with caveolin-1, but also for PAFR-mediated signaling, leading to IP production and MAPK activation.…”

Section: Discussionmentioning

confidence: 50%

Caveolae Facilitate but Are Not Essential for Platelet-Activating Factor-Mediated Calcium Mobilization and Extracellular Signal-Regulated Kinase Activation

Poisson

Rollin

Véronneau

et al. 2009

The Journal of Immunology

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Certain proteins, including receptors and signaling molecules, are known to be enriched in caveolae and lipid rafts. Caveolin-1, the major structural protein of caveolae, specifically interacts with many signaling molecules and, thus, caveolae and lipid rafts are often seen as preassembled signaling platforms. A potential binding site for caveolin-1 is present in the platelet-activating factor receptor (PAFR) sequence, and many downstream signaling components of PAFR activation preferentially localize in caveolae. The aim of this study was to investigate whether the PAFR was localized in caveolae/lipid raft domains and, if so, what would be the significance of such localization for PAFR signaling. In this study, we demonstrate that PAFR localizes within membrane microdomains, in close proximity to caveolin-1 in living cells, with potential interaction through a caveolin-1-binding sequence in the PAFR C terminus. Caveolin-1, however, is not essential for PAFR localization in lipid rafts. Disruption of caveolae/lipid rafts with methyl-β-cyclodextrin markedly reduced PAF-triggered inositol phosphate production and cytosolic calcium flux, suggesting that PAFR signaling through the Gαq protein was critically dependent on integrity of lipid rafts and/or caveolae. Interestingly, whereas in caveolin-1-expressing cells lipid raft disruption markedly decreased PAFR-mediated activation of the ERK/MAPK pathway, in cells lacking caveolae, such as leukocytes, lipid raft disruption had either the same inhibitory effect (Ramos B cells) or no effect (monocytes) on PAFR capacity to signal through the ERK/MAPK pathway. In conclusion, PAFR appears to localize within caveolae or lipid rafts in different cell types, and this location may be important for specific signaling events.

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A Polyaromatic Caveolin-Binding-Like Motif in the Cytoplasmic Tail of the Type 1 Receptor for Angiotensin II Plays an Important Role in Receptor Trafficking and Signaling

Cited by 82 publications

References 38 publications

The multi‐faceted cross‐talk between the insulin and angiotensin II signaling systems

The multi‐faceted cross‐talk between the insulin and angiotensin II signaling systems

Chemokine receptor internalization and intracellular trafficking

Caveolae Facilitate but Are Not Essential for Platelet-Activating Factor-Mediated Calcium Mobilization and Extracellular Signal-Regulated Kinase Activation

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