ArticleBiochemistry2012
Structural characterization of the caveolin scaffolding domain in association with cholesterol-rich membranes.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Article
- Membrane remodeling by the caveolin-1 8s oligomeric complex.Biophysical journal · 2025Article
- The role of transcytosis in the blood-retina barrier: from pathophysiological functions to drug delivery.Frontiers in pharmacology · 2025Review
- Ago2/CAV1 interaction potentiates metastasis via controlling Ago2 localization and miRNA action.EMBO reports · 2024Article
- Scaffolds and the scaffolding domain: an alternative paradigm for caveolin-1 signaling.Biochemical Society transactions · 2024Review
- Caveolin 1 Regulates the Tight Junctions between Sertoli Cells and Promotes the Integrity of Blood-Testis Barrier in Yak via the FAK/ERK Signaling Pathway.Animals : an open access journal from MDPI · 2024Article
- The Role of Membrane Lipids in the Formation and Function of Caveolae.Cold Spring Harbor perspectives in biology · 2023Review
- 3D-Printable centrifugal devices for biomolecular solid state NMR rotors.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Biochemical and Biophysical Characterization of the Caveolin-2 Interaction with Membranes and Analysis of the Protein Structural Alteration by the Presence of Cholesterol.International journal of molecular sciences · 2022Article
- Redox Regulation of Signaling Complex between Caveolin-1 and Neuronal Calcium Sensor Recoverin.Biomolecules · 2022Article
- Caveolar and non-Caveolar Caveolin-1 in ocular homeostasis and disease.Progress in retinal and eye research · 2022Review
- Article
- Molecular Mechanisms Underlying Caveolin-1 Mediated Membrane Curvature.The Journal of membrane biology · 2022Review
- Targeting Caveolin-1 and Claudin-5 with AY9944, Improve Blood-Brain Barrier Permeability; Computational Simulation and Experimental Study.Cellular and molecular neurobiology · 2022Article
- Caveolin-1-Derived Peptide Reduces ER Stress and Enhances Gelatinolytic Activity in IPF Fibroblasts.International journal of molecular sciences · 2022Article
- S-palmitoylation and sterol interactions mediate antiviral specificity of IFITM isoforms.Research square · 2021Article
- Reconstitution of Caveolin-1 into Artificial Lipid Membrane: Characterization by Transmission Electron Microscopy and Solid-State Nuclear Magnetic Resonance.Molecules (Basel, Switzerland) · 2021Article
- NMR identification of a conserved Drp1 cardiolipin-binding motif essential for stress-induced mitochondrial fission.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Single molecule network analysis identifies structural changes to caveolae and scaffolds due to mutation of the caveolin-1 scaffolding domain.Scientific reports · 2021Article
- Caveolin-1 Regulates Cellular Metabolism: A Potential Therapeutic Target in Kidney Disease.Frontiers in pharmacology · 2021Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Members of the caveolin protein family are implicated in the formation of caveolae and play important roles in a number of signaling pathways and in the regulation of various proteins. We employ complementary spectroscopic methods to study the structure of the caveolin scaffolding domain (CSD) in caveolin-1 fragments, while bound to cholesterol-rich membranes. This key domain is thought to be involved in multiple critical functions that include protein recognition, oligomerization, and cholesterol binding. In our membrane-bound peptides, residues within the flanking intramembrane domain (IMD) are found to adopt an α-helical structure, consistent with its commonly believed helical hairpin conformation. Intriguingly, in these same peptides, we observe a β-stranded conformation for residues in the CSD, contrasting with earlier reports, which commonly do not reflect β-structure. Our experimental data based on solid-state NMR, CD, and FTIR are found to be consistent with computational analyses of the secondary structure preference of the primary sequence. We discuss how our structural data of membrane binding Cav fragments may match certain general features of cholesterol-binding domains and could be consistent with the role for CSD in protein recognition and homo-oligomerization.
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Registered trials
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