期刊
CELL CHEMICAL BIOLOGY
卷 27, 期 8, 页码 1097-+出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2020.07.017
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资金
- Swiss National Foundation Sinergia [CRSII5_170925]
- Swiss National Science Foundation (SNF) [CRSII5_170925] Funding Source: Swiss National Science Foundation (SNF)
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 Jacking 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-InsP(5). 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-InsP(5) and central cellular regulators, such as lipid phosphatases, protein kinases, and GTPases, and identified protein domains commonly targeted by 5PP-InsP(5). 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.
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