Proteome-Wide Characterizations of N⁶-Methyl-Adenosine Triphosphate- and N⁶-Furfuryl-Adenosine Triphosphate-Binding Capabilities of Kinases.

ABSTRACT: Kinases catalyze the transfer of the γ-phosphate group from adenosine triphosphate (ATP) to their protein and small-molecule substrates, and this phosphorylation is a crucial element of multiple cell signaling pathways. Herein, we employed isotope-coded ATP acyl-phosphate probes, in conjunction with a multiple-reaction monitoring (MRM)-based targeted proteomic method for proteome-wide identifications of endogenous kinases that can bind to two N⁶-modified ATP derivatives, N⁶-methyl-ATP (N⁶-Me-ATP), and N⁶-furfuryl-ATP (a.k.a. kinetin triphosphate, KTP). We found that, among the ∼300 quantified kinases, 27 and 18 are candidate kinases that can bind to KTP and N⁶-Me-ATP, respectively. Additionally, GSK3α

SUBMITTER: Dong X 

PROVIDER: S-EPMC8809106 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature