ArticleThe Journal of biological chemistry2010
The role of proline in the membrane re-entrant helix of caveolin-1.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 43 citations in OpenAlex.
- Navigating lipid droplet proteins - part II: molecular mechanisms underlying ER-to-lipid droplet protein partitioning.Biochemical Society transactions · 2025Review
- Navigating lipid droplet proteins - part I: ER targeting routes of lipid droplet-destined membrane proteins.Biochemical Society transactions · 2025Review
- Membrane remodeling by the caveolin-1 8s oligomeric complex.Biophysical journal · 2025Article
- Caveolin-1: an ambiguous entity in breast cancer.Molecular cancer · 2025Review
- Are There Lipid Membrane-Domain Subtypes in Neurons with Different Roles in Calcium Signaling?Molecules (Basel, Switzerland) · 2023Review
- 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
- Molecular Mechanisms Underlying Caveolin-1 Mediated Membrane Curvature.The Journal of membrane biology · 2022Review
- ANKRD22 is an N-myristoylated hairpin-like monotopic membrane protein specifically localized to lipid droplets.Scientific reports · 2021Article
- Caveolin1 Tyrosine-14 Phosphorylation: Role in Cellular Responsiveness to Mechanical Cues.The Journal of membrane biology · 2020Review
- Interplay between Membrane Curvature and Cholesterol: Role of Palmitoylated Caveolin-1.Biophysical journal · 2019Article
- Article
- Membrane association of monotopic phosphoglycosyl transferase underpins function.Nature chemical biology · 2018Article
- Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Caveolins and cavins in the trafficking, maturation, and degradation of caveolae: implications for cell physiology.American journal of physiology. Cell physiology · 2017Review
- Article
- Probing the structure and dynamics of caveolin-1 in a caveolae-mimicking asymmetric lipid bilayer model.European biophysics journal : EBJ · 2016Article
- Reconstitution and spectroscopic analysis of caveolin-1 residues 62-178 reveals that proline 110 governs its structure and solvent exposure.Biochimica et biophysica acta · 2016Article
- Dictyostelium lipid droplets host novel proteins.Eukaryotic cell · 2013Article
- Characterization of the molecular architecture of human caveolin-3 and interaction with the skeletal muscle ryanodine receptor.The Journal of biological chemistry · 2012Article
- The transmembrane domain of caveolin-1 exhibits a helix-break-helix structure.Biochimica et biophysica acta · 2012Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caveolin-1 has a segment of hydrophobic amino acids comprising approximately residues 103-122. We have performed an in silico analysis of the conformational preference of this segment of caveolin-1 using PepLook. We find that there is one main group of stable conformations corresponding to a hydrophobic U bent model that would not traverse the membrane. Furthermore, the calculations predict that substituting the Pro(110) residue with an Ala will change the conformation to a straight hydrophobic helix that would traverse the membrane. We have expressed the P110A mutant of caveolin-1, with a FLAG tag at the N terminus, in HEK 293 cells. We evaluate the topology of the proteins with confocal immunofluorescence microscopy in these cells. We find that FLAG tag at the N terminus of the wild type caveolin-1 is not reactive with antibodies unless the cell membrane is permeabilized with detergent. This indicates that in these cells, the hydrophobic segment of this protein is not transmembrane but takes up a bent conformation, making the protein monotopic. In contrast, the FLAG tag at the N terminus of the P110A mutant is equally exposed to antibodies, before and after membrane permeabilization. We also find that the P110A mutation causes a large reduction of endocytosis of caveolae, cellular lipid accumulation, and lipid droplet formulation. In addition, we find that this mutation markedly reduces the ability of caveolin-1 to form structures with the characteristic morphology of caveolae or to partition into the detergent-resistant membranes of these cells. Thus, the single Pro residue in the membrane-inserting segment of caveolin-1 plays an important role in both the membrane topology and localization of the protein as well as its functions.
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