ArticleNature communications2025
The molecular basis of Human FN3K mediated phosphorylation of glycated substrates.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- N4BP1 uses tandem KH domains to associate with EDC4 and mRNA decapping factors in P-bodies.Communications biology · 2026Article
- Protein turnover in plants-cost of synthesis, repair, and crop engineering opportunities.Plant physiology · 2026Review
- Article
- Ancestral protein reconstruction reveals the mechanism of substrate specificity in FN3K-mediated deglycation.Communications biology · 2026Article
- FN3K deficiency drives tubular injury in diabetic kidney disease through impaired mitochondrial respiratory chain function.Frontiers in endocrinology · 2026Article
- Ancestral protein reconstruction reveals the mechanism of substrate specificity in FN3K-mediated deglycation.Research square · 2025Article
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7 authors.
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Abstract
Glycation, a non-enzymatic post-translational modification occurring on proteins, can be actively reversed via site-specific phosphorylation of the fructose-lysine moiety by FN3K kinase, to impact the cellular function of the target protein. A regulatory axis between FN3K and glycated protein targets has been associated with conditions like diabetes and cancer. However, the molecular basis of this relationship has not been explored so far. Here, we determined a series of crystal structures of HsFN3K in the apo-state, and in complex with different nucleotide analogs together with a sugar substrate mimic to reveal the features important for its kinase activity and substrate recognition. Additionally, the dynamics in sugar substrate binding during the kinase catalytic cycle provide important mechanistic insights into HsFN3K function. Our structural work provides the molecular basis for rational small molecule design targeting FN3K.
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