An Affinity-Based, Cysteine-Specific ATP Analog for Kinase-Catalyzed Crosslinking.

ABSTRACT: Kinases mediate cell signaling pathways by catalyzing protein phosphorylation. Irregularities in kinase activity are directly associated with disease conditions. Therefore, methods to identify substrates of a particular kinase are needed to understand signaling cascades in normal and diseased states. Photocrosslinking ATP analogs provide powerful tools to study kinases by covalently linking kinases with substrates. However, the involvement of UV light and nonspecific reactivity of current ATP-photocrosslinkers challenge kinase-substrate identification. We report here an affinity-based crosslinking ATP analog, ATP-methylacrylamide (ATP-MAc), that contains a cysteine-reactive acrylamide crosslinking group, which avoids the UV irradiation and non-specific reactivity of prior analogs. Using in

SUBMITTER: Fouda AE 

PROVIDER: S-EPMC8084585 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature