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- W3048708568 abstract "The inositol pyrophosphates (PP-InsPs) are a ubiquitous group of highly phosphorylated eukaryotic messengers. They have been linked to a panoply of central cellular processes, but a detailed understanding of the discrete signaling events is lacking in most cases. To create a more mechanistic picture of PP-InsP signaling, we sought to annotate the mammalian interactome of the most abundant inositol pyrophosphate 5PP-InsP5. To do so, triplexed affinity reagents were developed, in which a metabolically stable PP-InsP analog was immobilized in three different ways. Application of these triplexed reagents to mammalian lysates identified between 300 and 400 putative interacting proteins. These interactomes revealed connections between 5PP-InsP5 and central cellular regulators, such as lipid phosphatases, protein kinases, and GTPases, and identified protein domains commonly targeted by 5PP-InsP5. Both the triplexed affinity reagents, and the proteomic datasets, constitute powerful resources for the community, to launch future investigations into the multiple signaling modalities of inositol pyrophosphates." @default.
- W3048708568 created "2020-08-18" @default.
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- W3048708568 date "2020-08-01" @default.
- W3048708568 modified "2023-10-17" @default.
- W3048708568 title "Triplexed Affinity Reagents to Sample the Mammalian Inositol Pyrophosphate Interactome" @default.
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- W3048708568 doi "https://doi.org/10.1016/j.chembiol.2020.07.017" @default.
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