Structure-Based Reassessment of the Caveolin Signaling Model: Do Caveolae Regulate Signaling through Caveolin-Protein Interactions?

被引：113

作者：

Collins, Brett M. ^{[1
]}

Davis, Melissa J. ^{[1
,3
]}

Hancock, John F. ^{[4
]}

Parton, Robert G. ^{[1
,2
]}

机构：

[1] Univ Queensland, Inst Mol Biosci, Brisbane, Qld 4072, Australia

[2] Univ Queensland, Ctr Microscopy & Microanal, Brisbane, Qld 4072, Australia

[3] Univ Queensland, Queensland Facil Adv Bioinformat, Brisbane, Qld 4072, Australia

[4] Univ Texas Hlth Sci Ctr, Dept Integrat Biol & Pharmacol, Houston, TX 77030 USA

来源：

DEVELOPMENTAL CELL | 2012年 / 23卷 / 01期

基金：

英国医学研究理事会; 澳大利亚研究理事会; 美国国家卫生研究院; 澳大利亚国家健康与医学研究理事会;

关键词：

NITRIC-OXIDE SYNTHASE; TYROSINE KINASE DOMAIN; NICOTINIC ACETYLCHOLINE-RECEPTOR; HIV-1 GLYCOPROTEIN GP41; MURINE LEUKEMIA-VIRUS; CRYSTAL-STRUCTURE; SCAFFOLDING DOMAIN; BINDING DOMAIN; ANGSTROM RESOLUTION; PLASMA-MEMBRANE;

D O I：

10.1016/j.devcel.2012.06.012

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页码：11 / 20

页数：10

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