Genetic and biochemical analysis of two enzymes reveals that inositol pyrophosphate signaling molecules allow plants to sense and regulate cellular phosphate levels, and to take up more phosphate when needed.

Analysis of inositol pyrophosphate dynamics upon inorganic phosphate (P_i) starvation identifies 1,5-IP₈ as the inositol pyrophosphate isomer signaling P_i sufficiency to the SPX domain of Pho81 that controls the transcriptional P_i starvation program.

Structural and biochemical data suggest a mechanism for the Synaptojanin1-catalysed reaction and the role of mutations in the onset of associated neurological diseases.

The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its function.

The inositol phosphate IP6 is selectively packaged into HIV virions, where it coordinates electropositive pores in the capsid to prevent spontaneous collapse and promote encapsidated DNA synthesis.

A high-phytate-low Ca²⁺ diet causes crystal nephropathies, renal phosphate wasting, and bone disease in rats, whereas high Ca²⁺ intake ameliorates the detrimental effects of a high-phytate diet.

PIP₂ inhibits the proton-activated chloride (PAC) channel by selectively stabilizing its desensitized state.

PPM1H protein phosphatase dephosphorylates Rab proteins modulating LRRK2 signalling.

A theoretical conceptualization of how phosphates control metabolic information flow and predictably regulate the metabolic state of the cell.

C-terminal phosphorylation of the lipid phosphatase PTEN drives a reduction in membrane affinity and leads to a more compact conformation that involves a C2 domain-tail interaction.