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Updated: Oct 11, 2025

Preparation of Quality Inositol Pyrophosphates
Published on: September 3, 2011
Secreted acid phosphatases maintain replicative lifespan via inositol polyphosphate metabolism in budding yeast
Toshio Nakajima1, Shun Hosoyamada2, Takehiko Kobayashi2,3
1Department of Frontier Bioscience, Nagahama Institute of Bio-Science and Technology, Shiga, Japan.
Abstract:
Secreted acid phosphatases (APases) dephosphorylate extracellular organic phosphate compounds to supply inorganic phosphate (Pi) to maintain cellular functions. Here, we show that APases are necessary to maintain a normal replicative lifespan in Saccharomyces cerevisiae. Deletion of all four APase genes shortened the lifespan in yeast strains on synthetic media (irrespective of the concentrations of Pi in the media), but it did not affect the intracellular ortho- and polyphosphate levels. Deletion of inositol-pentakisphosphate 2-kinase (IPK1), which encodes inositol-pentakisphosphate 2-kinase, restored the lifespan in APase-null mutants, and IPK1 overexpression shortened the lifespan in wild-type strains. Overexpression of inositol hexakisphosphate (IP6 ) and heptakisphosphate kinases, KCS1 and VIP1, recovered the lifespan in APase-null mutants. Thus, yeast APases modulate the replicative lifespan, probably through dephosphorylation of intracellular IP6 .
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