ArticleBiochimica et biophysica acta2012
Acetylation of αA-crystallin in the human lens: effects on structure and chaperone function.
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 40 papers.
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Who cites it
40 citing papers in PubMed, 72 citations in OpenAlex.
- HuD and alpha-crystallin A axis protects neuro-retinal cells in early diabetes.Molecular and cellular biochemistry · 2025Article
- Proteomic Characterization of the Rhesus Macaque Lens Nucleus: Similarity to Human Lens, Age Effects on Protein Solubility, and Trends in Post-Translational Modifications.Investigative ophthalmology & visual science · 2025Article
- Aquaporin-0-protein interactions elucidated by crosslinking mass spectrometry.Biochemical and biophysical research communications · 2024Article
- Thiol-Mediated Enhancement of NACS chemical biology · 2024Article
- Tissue, cellular, and molecular level determinants for eye lens stiffness and elasticity.Frontiers in ophthalmology · 2024Review
- Article
- Promotion of Protein Solubility and Reduction in Stiffness in Human Lenses by Aggrelyte-1: Implications for Reversing Presbyopia.International journal of molecular sciences · 2023Article
- Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens.The Journal of biological chemistry · 2022Review
- Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens.International journal of molecular sciences · 2022Article
- Small Heat Shock Proteins in Retinal Diseases.Frontiers in molecular biosciences · 2022Review
- A direct nuclear magnetic resonance method to investigate lysine acetylation of intrinsically disordered proteins.Frontiers in molecular biosciences · 2022Article
- Minimal Yet Powerful: The Role of Archaeal Small Heat Shock Proteins in Maintaining Protein Homeostasis.Frontiers in molecular biosciences · 2022Review
- Therapeutic Potential of α-Crystallins in Retinal Neurodegenerative Diseases.Antioxidants (Basel, Switzerland) · 2021Review
- Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation.Membranes · 2021Review
- Proteomic characterization of the human lens and Cataractogenesis.Expert review of proteomics · 2021Review
- Chaperone client proteins evolve slower than non-client proteins.Functional & integrative genomics · 2020Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- Lysine malonylation and propionylation are prevalent in human lens proteins.Experimental eye research · 2020Article
- The absence of SIRT3 and SIRT5 promotes the acetylation of lens proteins and improves the chaperone activity of α-crystallin in mouse lenses.Experimental eye research · 2019Article
- A monoclonal antibody targeted to the functional peptide of αB-crystallin inhibits the chaperone and anti-apoptotic activities.Journal of immunological methods · 2019Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
α-Crystallin is a major protein in the human lens that is perceived to help to maintain the transparency of the lens through its chaperone function. In this study, we demonstrate that many lens proteins including αA-crystallin are acetylated in vivo. We found that K70 and K99 in αA-crystallin and, K92 and K166 in αB-crystallin are acetylated in the human lens. To determine the effect of acetylation on the chaperone function and structural changes, αA-crystallin was acetylated using acetic anhydride. The resulting protein showed strong immunoreactivity against a N(ε)-acetyllysine antibody, which was directly related to the degree of acetylation. When compared to the unmodified protein, the chaperone function of the in vitro acetylated αA-crystallin was higher against three of the four different client proteins tested. Because a lysine (residue 70; K70) in αA-crystallin is acetylated in vivo, we generated a protein with an acetylation mimic, replacing Lys70 with glutamine (K70Q). The K70Q mutant protein showed increased chaperone function against three client proteins compared to the Wt protein but decreased chaperone function against γ-crystallin. The acetylated protein displayed higher surface hydrophobicity and tryptophan fluorescence, had altered secondary and tertiary structures and displayed decreased thermodynamic stability. Together, our data suggest that acetylation of αA-crystallin occurs in the human lens and that it affects the chaperone function of the protein.
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