ArticleProtein engineering, design & selection : PEDS2016
Fully reduced granulin-B is intrinsically disordered and displays concentration-dependent dynamics.
Article in Protein engineering, design & selection : PEDS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- The C-terminal region ofAustralian journal of chemistry · 2025Article
- Reversible Disulfide Bond Cross-Links as Tunable Levers of Phase Separation in Designer Biomolecular Condensates.Journal of the American Chemical Society · 2024Article
- Are granulins copper sequestering proteins?Proteins · 2021Article
- Fatal Attraction: The Case of Toxic Soluble Dimers of Truncated PQBP-1 Mutants in X-Linked Intellectual Disability.International journal of molecular sciences · 2021Review
- Folding of Truncated Granulin Peptides.Biomolecules · 2020Article
- Granulins modulate liquid-liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43.The Journal of biological chemistry · 2020Article
- Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions.Progress in molecular biology and translational science · 2020Review
- Cysteine-rich granulin-3 rapidly promotes amyloid-β fibrils in both redox states.The Biochemical journal · 2019Article
- Structural Variants of a Liver Fluke Derived Granulin Peptide Potently Stimulate Wound Healing.Journal of medicinal chemistry · 2018Article
- Structure dissection of zebrafish progranulins identifies a well-folded granulin/epithelin module protein with pro-cell survival activities.Protein science : a publication of the Protein Society · 2018Article
- Disulfide bonds and disorder in granulin-3: An unusual handshake between structural stability and plasticity.Protein science : a publication of the Protein Society · 2017Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Granulins (Grns) are a family of small, cysteine-rich proteins that are generated upon proteolytic cleavage of their precursor, progranulin (Pgrn). All seven Grns (A-G) contain 12 conserved cysteines that form 6 intramolecular disulfide bonds, rendering this family of proteins unique. Grns are known to play multi-functional roles, including wound healing, embryonic growth, and inflammation and are implicated in neurodegenerative diseases. Despite their manifold functions, there exists a dearth of information regarding their structure-function relationship. Here, we sought to establish the role of disulfide bonds in promoting structure by investigating the fully reduced GrnB (rGrnB). We report that monomeric rGrnB is an intrinsically disordered protein (IDP) at low concentrations. rGrnB undergoes dimerization at higher concentrations to form a fuzzy complex without a net gain in the structure-a behavior increasingly identified as a hallmark of some IDPs. Interestingly, we show that rGrnB is also able to activate NF-κB in human neuroblastoma cells in a concentration-dependent manner. This activation correlates with the observed monomer-dimer dynamics. Collectively, the presented data establish that the intrinsic disorder of rGrnB governs conformational dynamics within the reduced form of the protein, and suggest that the overall structure of Grns could be entirely dictated by disulfide bonds.
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Registered trials
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