Back on the chain gang: polyphosphate modification of proteins

Nolan Neville; Kirsten Lehotsky; Zongchao Jia

doi:10.1016/j.tibs.2024.06.010

Back on the chain gang: polyphosphate modification of proteins

Trends Biochem Sci. 2024 Sep;49(9):757-760. doi: 10.1016/j.tibs.2024.06.010. Epub 2024 Jun 29.

Authors

Nolan Neville¹, Kirsten Lehotsky¹, Zongchao Jia²

Affiliations

¹ Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6, Canada.
² Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6, Canada. Electronic address: jia@queensu.ca.

PMID: 38945730
DOI: 10.1016/j.tibs.2024.06.010

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.

Keywords: PASK; histidine repeat; lysine repeat; polyphosphate; polyphosphorylation.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

Humans
Polyphosphates* / chemistry
Polyphosphates* / metabolism
Proteins* / chemistry
Proteins* / metabolism

Substances

Polyphosphates
Proteins