ArticleBiochemical and biophysical research communications2017
The regulatory α and β subunits of phosphorylase kinase directly interact with its substrate, glycogen phosphorylase.
Article in Biochemical and biophysical research communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Diabetic Polyneuropathy Patients Exhibit an Altered Skeletal Muscle Proteome Phenotype.Proteomics. Clinical applications · 2026Article
- Chrono overexpression blunts exercise-induced improvement in muscular glucose metabolism by inhibiting the BMAL1 transcriptional activity in high-fat diet-fed mice.Journal of physiology and biochemistry · 2026Article
- Molecular basis for the regulation of human phosphorylase kinase by phosphorylation and CaNature communications · 2025Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
The selective phosphorylation of glycogen phosphorylase (GP) by its only known kinase, phosphorylase kinase (PhK), keeps glycogen catabolism tightly regulated. In addition to the obligatory interaction between the catalytic γ subunit of PhK and the phosphorylatable region of GP, previous studies have suggested additional sites of interaction between this kinase and its protein substrate. Using short chemical crosslinkers, we have identified direct interactions of GP with the large regulatory α and β subunits of PhK. These newfound interactions were found to be sensitive to ligands that bind PhK.
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