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O'Shea Lab > People > Kristen Cook

 

Inositol phosphate signaling in the PHO pathway of S. cerevisiae
Recent work from our lab has shown that the inhibition of Pho80/85 requires IP7 (Lee, Mulugu et al. 2007). When cells are starved of phosphate, IP7 levels increase. IP7 then physically interacts wi th the CDK inhibitor (CKI) Pho81, triggering inhibition of Pho80/85. Although the biochemical connection between increased IP7 and PHO pathway activation is clear, we do not understand how cells sense changes in phosphate availability and modulate IP7 levels accordingly. By studying this system in detail, we can generate a complete description of the function and mechanism of an inositol pyrophosphate signal, within the context of a well-understood biological response. To determine how IP7 is regulated in response to phosphate availability, I am studying the enzymes involved in production and destruction of IP7.

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