Molecular characterization of caveolin-induced membrane curvature

Ariotti, Nicholas, Rae, James, Leneva, Natalya, Ferguson, Charles, Loo, Dorothy, Okano, Satomi, Hill, Michelle M., Walser, Piers, Collins, Brett M. and Parton, Robert G. (2015) Molecular characterization of caveolin-induced membrane curvature. Journal of Biological Chemistry, 290 41: 24875-24890. doi:10.1074/jbc.M115.644336

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Author Ariotti, Nicholas
Rae, James
Leneva, Natalya
Ferguson, Charles
Loo, Dorothy
Okano, Satomi
Hill, Michelle M.
Walser, Piers
Collins, Brett M.
Parton, Robert G.
Title Molecular characterization of caveolin-induced membrane curvature
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 1083-351X
Publication date 2015-10-09
Sub-type Article (original research)
DOI 10.1074/jbc.M115.644336
Open Access Status File (Publisher version)
Volume 290
Issue 41
Start page 24875
End page 24890
Total pages 16
Place of publication Rockville, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2016
Language eng
Abstract The generation of caveolae involves insertion of the cholesterol-binding integral membrane protein caveolin-1 (Cav1) into the membrane, however, the precise molecular mechanisms are as yet unknown. We have speculated that insertion of the caveolin scaffolding domain (CSD), a conserved amphipathic region implicated in interactions with signaling proteins, is crucial for caveola formation. We now define the core membrane-juxtaposed region of Cav1 and show that the oligomerization domain and CSD are protected by tight association with the membrane in both mature mammalian caveolae and a model prokaryotic system for caveola biogenesis. Cryoelectron tomography reveals the core membrane-juxtaposed domain to be sufficient to maintain oligomerization as defined by polyhedral distortion of the caveolar membrane. Through mutagenesis we demonstrate the importance of the membrane association of the oligomerization domain/CSD for defined caveola biogenesis and furthermore, highlight the functional significance of the intramembrane domain and the CSD for defined caveolin-induced membrane deformation. Finally, we define the core structural domain of Cav1, constituting only 66 amino acids and of great potential to nanoengineering applications, which is required for caveolin-induced vesicle formation in a bacterial system. These results have significant implications for understanding the role of Cav1 in caveola formation and in regulating cellular signaling events.
Keyword Caveolae
Electron microscopy (EM)
Electron tomography
Protein domain
Membrane deformation
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

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