Chemical proteomics reveals interactors of the alarmone diadenosine triphosphate in the cancer cell line H1299.

Intracellular dinucleoside polyphosphates (Np Ns) have been known for decades but the functional role remains enigmatic. Diadenosine triphosphate (Ap A) is one of the most prominent examples, and its intercellular concentration was shown to increase upon cellular stress. By employment of previously reported Ap A-based photoaffinity-labeling probes (PALPs) in chemical proteomics, we investigated the Ap A interactome in the human lung carcinoma cell line H1299.

Chemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate.

The nucleotides diadenosine triphosphate (ApA) and diadenosine tetraphosphate (ApA) are formed in prokaryotic and eukaryotic cells. Since their concentrations increase significantly upon cellular stress, they are considered to be alarmones triggering stress adaptive processes. However, their cellular roles remain elusive.