ArticleBiochimica et biophysica acta2012
The transmembrane domain of caveolin-1 exhibits a helix-break-helix structure.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 58 citations in OpenAlex.
- Navigating lipid droplet proteins - part I: ER targeting routes of lipid droplet-destined membrane proteins.Biochemical Society transactions · 2025Review
- A model for membrane curvature generation by caveolin discs driven by differential contact interaction.Nature communications · 2025Article
- Membrane remodeling by the caveolin-1 8s oligomeric complex.Biophysical journal · 2025Article
- Caveolin assemblies displace one bilayer leaflet to organize and bend membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Caveolin assemblies displace one bilayer leaflet to organize and bend membranes.bioRxiv : the preprint server for biology · 2025Article
- Scaffolds and the scaffolding domain: an alternative paradigm for caveolin-1 signaling.Biochemical Society transactions · 2024Review
- Are There Lipid Membrane-Domain Subtypes in Neurons with Different Roles in Calcium Signaling?Molecules (Basel, Switzerland) · 2023Review
- Simulations suggest a scaffolding mechanism of membrane deformation by the caveolin 8S complex.Biophysical journal · 2023Article
- The Role of Membrane Lipids in the Formation and Function of Caveolae.Cold Spring Harbor perspectives in biology · 2023Review
- The building blocks of caveolae revealed: caveolins finally take center stage.Biochemical Society transactions · 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
- Emerging Insights into the Molecular Architecture of Caveolin-1.The Journal of membrane biology · 2022Review
- Molecular Mechanisms Underlying Caveolin-1 Mediated Membrane Curvature.The Journal of membrane biology · 2022Review
- Molecular architecture of the human caveolin-1 complex.Science advances · 2022Article
- Structural Interplays in the Flexible N-Terminus and Scaffolding Domain of Human Membrane Protein Caveolin 3.Membranes · 2021Article
- Caveolin1 Tyrosine-14 Phosphorylation: Role in Cellular Responsiveness to Mechanical Cues.The Journal of membrane biology · 2020Review
- Structure and assembly of CAV1 8S complexes revealed by single particle electron microscopy.Science advances · 2020Article
- Reconstitution of full-length human caveolin-1 into phospholipid bicelles: Validation by analytical ultracentrifugation.Biophysical chemistry · 2020Article
- U-shaped caveolin-1 conformations are tightly regulated by hydrogen bonds with lipids.Journal of computational chemistry · 2019Article
- Interplay between Membrane Curvature and Cholesterol: Role of Palmitoylated Caveolin-1.Biophysical journal · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Caveolin is an integral membrane protein that is found in high abundance in caveolae. Both the N- and C- termini lie on the same side of the membrane, and the transmembrane domain has been postulated to form an unusual intra-membrane horseshoe configuration. To probe the structure of the transmembrane domain, we have prepared a construct of caveolin-1 that encompasses residues 96-136 (the entire intact transmembrane domain). Caveolin-1(96-136) was over-expressed and isotopically labeled in E. coli, purified to homogeneity, and incorporated into lyso-myristoylphosphatidylglycerol micelles. Circular dichroism and NMR spectroscopy reveal that the transmembrane domain of caveolin-1 is primarily α-helical (57-65%). Furthermore, chemical shift indexing reveals that the transmembrane domain has a helix-break-helix structure which could be critical for the formation of the intra-membrane horseshoe conformation predicted for caveolin-1. The break in the helix spans residues 108 to 110, and alanine scanning mutagenesis was carried out to probe the structural significance of these residues. Our results indicate that mutation of glycine 108 to alanine does not disrupt the structure, but mutation of isoleucine 109 and proline 110 to alanine dramatically alters the helix-break-helix structure. To explore the structural determinants further, additional mutagenesis was performed. Glycine 108 can be substituted with other small side chain amino acids (i.e. alanine), leucine 109 can be substituted with other β-branched amino acids (i.e. valine), and proline 110 cannot be substituted without disrupting the helix-break-helix structure.
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