ArticleBiochemistry2012
Probing the caveolin-1 P132L mutant: critical insights into its oligomeric behavior and structure.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Scaffolds and the scaffolding domain: an alternative paradigm for caveolin-1 signaling.Biochemical Society transactions · 2024Review
- One-step site-specific S-alkylation of full-length caveolin-1: Lipidation modulates the topology of its C-terminal domain.Protein science : a publication of the Protein Society · 2023Article
- Template-free prediction of a new monotopic membrane protein fold and assembly by AlphaFold2.Biophysical journal · 2023Article
- The building blocks of caveolae revealed: caveolins finally take center stage.Biochemical Society transactions · 2023Article
- Stromal Fibroblasts Counteract the Caveolin-1-Dependent Radiation Response of LNCaP Prostate Carcinoma Cells.Frontiers in oncology · 2022Article
- Reconstitution of Caveolin-1 into Artificial Lipid Membrane: Characterization by Transmission Electron Microscopy and Solid-State Nuclear Magnetic Resonance.Molecules (Basel, Switzerland) · 2021Article
- Structural Interplays in the Flexible N-Terminus and Scaffolding Domain of Human Membrane Protein Caveolin 3.Membranes · 2021Article
- Reconstitution of full-length human caveolin-1 into phospholipid bicelles: Validation by analytical ultracentrifugation.Biophysical chemistry · 2020Article
- Ascidian caveolin induces membrane curvature and protects tissue integrity and morphology during embryogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Efficient solubilization and purification of highly insoluble membrane proteins expressed as inclusion bodies using perfluorooctanoic acid.Protein expression and purification · 2018Article
- A pH-Mediated Topological Switch within the N-Terminal Domain of Human Caveolin-3.Biophysical journal · 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
- Assembly and Turnover of Caveolae: What Do We Really Know?Frontiers in cell and developmental biology · 2016Review
- Molecular Characterization of Caveolin-induced Membrane Curvature.The Journal of biological chemistry · 2015Article
- Tagging strategies strongly affect the fate of overexpressed caveolin-1.Traffic (Copenhagen, Denmark) · 2015Article
- Modest effects of lipid modifications on the structure of caveolin-3.Biochemistry · 2014Article
- Overexpression of caveolin-1 is sufficient to phenocopy the behavior of a disease-associated mutant.Traffic (Copenhagen, Denmark) · 2013Article
- Caveolin-1 as a promoter of tumour spreading: when, how, where and why.Journal of cellular and molecular medicine · 2013Review
- Expression of Caveolin-1 Is Associated With Thyroid Function in Patients With Human Papillary Thyroid Carcinoma.Dose-response : a publication of International Hormesis SocietyArticle
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Caveolin-1 is the most important protein found in caveolae, which are cell surface invaginations of the plasma membrane that act as signaling platforms. A single point mutation in the transmembrane domain of caveolin-1 (proline 132 to leucine) has deleterious effects on caveolae formation in vivo and has been implicated in various disease states, particularly aggressive breast cancers. Using a combination of gel filtration chromatography and analytical ultracentrifugation, we found that a fully functional construct of caveolin-1 (Cav1(62-178)) was a monomer in dodecylphosphocholine micelles. In contrast, the P132L mutant of Cav1(62-178) was dimeric. To explore the dimerization of the P132L mutant further, various truncated constructs (Cav1(82-178), Cav1(96-178), Cav1(62-136), Cav1(82-136), Cav1(96-136)) were prepared which revealed that oligomerization occurs in the transmembrane domain (residues 96-136) of caveolin-1. To characterize the mutant structurally, solution-state NMR experiments in lyso-myristoylphosphatidylglycerol were undertaken of the Cav1(96-136) P132L mutant. Chemical shift analysis revealed that, compared to the wild-type, helix 2 in the transmembrane domain was lengthened by four residues (wild-type, residues 111-129; mutant, residues 111-133), which corresponds to an extra turn in helix 2 of the mutant. Lastly, point mutations at position 132 of Cav1(62-178) (P132A, P132I, P132V, P132G, P132W, P132F) revealed that no other hydrophobic amino acid can preserve the monomeric state of Cav1(62-178), which indicates that proline 132 is critical in supporting proper caveolin-1 behavior.
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