PolyP chains can bind to protein targets at PASK, polyK and polyH motifs. Originally proposed as a covalent modification, our current model is that polyP interacts with proteins non-covalently. But, models are made to be broken!
Our work was featured on the cover of the March 27, 2018 edition of Cell Reports.
Polyphosphate Biology:
Polyphosphates (polyP) are chains of up to thousands of phosphate residues joined by high energy bonds. PolyP is found in most cells on earth, including bacteria, yeasts, and human cells. In microorganisms, polyP is thought to serve as an energy storage and a phosphate reserve, and may play a role in bacterial virulence, gene expression and stress responses. In mammalian cells, which contain much lower amounts of polyP than microorganisms, polyP impacts apoptosis, cell proliferation, energy metabolism, and blood clotting.
PolyP synthesis is achieved by polyphosphate kinases while polyphosphatases degrade polyP chains. We are interested in the regulation of these activities in different species. We are also very interested in the way that polyP interacts with proteins in the cell to regulate diverse aspects of cell homeostasis.
Relevant Papers:
Bentley-DeSousa et al. 2018; Bentley-DeSousa et al. 2019; Downey, 2019; McCarthy et al. 2020; Bondy-Chorney et al. 2020. Denoncourt et. al 2021, Baijal et al. 2021a Baijal et al. 2021b, Bentley-DeSousa et al. 2021, McCarthy et al. 2022, McCarthy et al. 2023, Neville et al. 2023, Baijal et a. 2024, Neville et al. 2024
Our work in the area of polyP uses bacterial, yeast, and cell culture models.
Our polyP work is funded through CIHR.
Watch an (old-ish) seminar of Mike talking about polyP