Back on the chain gang: polyphosphate modification of proteins.

Nolan Neville, Zongchao Jia, Kirsten Lehotsky

Journal: Trends in biochemical sciences 2024;49(9):757-760

PMID: 38945730

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Abstract

Polyphosphate (polyP) mediates a plethora of biological functions. Understanding the polyP-protein interactome will help clarify the mechanisms underpinning these functions. Recent studies demonstrating a strong but noncovalent modification of lysine and histidine repeat proteins by polyP have provided new insights into polyP-protein biochemistry with implications for research and therapeutics.

Address: Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6, Canada.; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6, Canada. Electronic address: [email protected].

DOI: 10.1016/j.tibs.2024.06.010

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MeSH Terms: Polyphosphates, Proteins, Humans