Journal
DEVELOPMENTAL CELL
Volume 23, Issue 1, Pages 11-20Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2012.06.012
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Funding
- Australian Research Council (ARC) [DP120101298, DP110103384, FT100100027]
- National Health and Medical Research Council (NHMRC) [APP1037320]
- NHMRC Australia [569542]
- National Institutes of Health [GM066717]
- Australian Research Council [FT100100027] Funding Source: Australian Research Council
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Caveolin proteins drive formation of caveolae, specialized cell-surface microdomains that influence cell signaling. Signaling proteins are proposed to use conserved caveolin-binding motifs (CBMs) to associate with caveolae via the caveolin scaffolding domain (CSD). However, structural and bioinformatic analyses argue against such direct physical interactions: in the majority of signaling proteins, the CBM is buried and inaccessible. Putative CBMs do not form a common structure for caveolin recognition, are not enriched among caveolin-binding proteins, and are even more common in yeast, which lack caveolae. We propose that CBM/CSD-dependent interactions are unlikely to mediate caveolar signaling, and the basis for signaling effects should therefore be reassessed.
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