ReviewProtein science : a publication of the Protein Society2021
Adenosine triphosphate energy-independently controls protein homeostasis with unique structure and diverse mechanisms.
Review in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 80 citations in OpenAlex.
- Electroacupuncture alleviates depressive symptoms in post-stroke depression rat models by AMPK-mediated mitochondrial pathway.Psychopharmacology · 2026Article
- Adenosine triphosphate as a modulator of protein interactions and stability.FEBS open bio · 2026Review
- ATP binding to lysozyme and superfolder GFP amyloid fibrils induces aggregate remodeling and attenuates their cytotoxicity.Cell death discovery · 2026Article
- Short autoinhibitory sequences control phase separation of an essential bacterial transcription termination factor.The EMBO journal · 2026Article
- Aggregation of Phosphates Enhances Enzyme Activity in Aqueous Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- ATP and small amphiphilic molecules act as molecular matchmakers to fine-tune FET protein clusters.Communications chemistry · 2025Article
- ATP Can Act as a Stabilizer on Neutral Macromolecules.The journal of physical chemistry letters · 2025Article
- The synaptic vesicle cluster as a controller of pre- and postsynaptic structure and function.The Journal of physiology · 2025Review
- Biomolecular phase separation in tumorigenesis: from aberrant condensates to therapeutic vulnerabilities.Molecular cancer · 2025Review
- Determining the Role of Electrostatics in the Making and Breaking of the Caprin1-ATP Nanocondensate.The journal of physical chemistry. B · 2025Article
- In the Beginning: Let Hydration Be Coded in Proteins for Manifestation and Modulation by Salts and Adenosine Triphosphate.International journal of molecular sciences · 2024Review
- Protective Effects of Food-Derived Kaempferol on Pancreatic β-Cells in Type 1 Diabetes Mellitus.Foods (Basel, Switzerland) · 2024Article
- Article
- Molecular Mechanisms of Phase Separation and Amyloidosis of ALS/FTD-linked FUS and TDP-43.Aging and disease · 2024Review
- NMR Dynamic View of the Stabilization of the WW4 Domain by Neutral NaCl and Kosmotropic NaInternational journal of molecular sciences · 2024Article
- Unraveling the Mechanisms of Efficient Phosphorus Utilization in Popcorn (Journal of proteome research · 2024Article
- NMR Dynamic View of the Destabilization of WW4 Domain by Chaotropic GdmCl and NaSCN.International journal of molecular sciences · 2024Article
- Adenosine Triphosphate: The Primordial Molecule That Controls Protein Homeostasis and Shapes the Genome-Proteome Interface.Biomolecules · 2024Review
- Mitochondrial Fission in Nickel Nanoparticle-Induced Reproductive Toxicity: An In Vitro GC-1 Cell Study.Nanomaterials (Basel, Switzerland) · 2024Article
- JunB condensation attenuates vascular endothelial damage under hyperglycemic condition.Journal of molecular cell biology · 2024Article
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1 author at 1 institution in 1 country.
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Abstract
Proteins function in the crowded cellular environments with high salt concentrations, thus facing tremendous challenges of misfolding/aggregation which represents a pathological hallmark of aging and an increasing spectrum of human diseases. Recently, intrinsically disordered regions (IDRs) were recognized to drive liquid-liquid phase separation (LLPS), a common principle for organizing cellular membraneless organelles (MLOs). ATP, the universal energy currency for all living cells, mysteriously has concentrations of 2-12 mM, much higher than required for its previously-known functions. Only recently, ATP was decoded to behave as a biological hydrotrope to inhibit protein LLPS and aggregation at mM. We further revealed that ATP also acts as a bivalent binder, which not only biphasically modulates LLPS driven by IDRs of human and viral proteins, but also bind to the conserved nucleic-acid-binding surfaces of the folded proteins. Most unexpectedly, ATP appears to act as a hydration mediator to antagonize the crowding-induced destabilization as well as to enhance folding of proteins without significant binding. Here, this review focuses on summarizing the results of these biophysical studies and discussing their implications in an evolutionary context. By linking triphosphate with unique hydration property to adenosine, ATP appears to couple the ability for establishing hydrophobic, π-π, π-cation and electrostatic interactions to the capacity in mediating hydration of proteins, which is at the heart of folding, dynamics, stability, phase separation and aggregation. Consequently, ATP acquired a category of functions at ~mM to energy-independently control protein homeostasis with diverse mechanisms, thus implying a link between cellular ATP concentrations and protein-aggregation diseases.
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