The apple palmitoyltransferase MdPAT16 regulates sugar content via an MdCBL1-MdCIPK13-MdSUT2.2 pathway

Abstract

Protein palmitoylation, a post-translational protein modification, plays an important role in the regulation of substrate protein stability, protein interactions, and protein localization. It is generally believed that there are two mechanisms of palmitoylation: one by acyl-CoA and the other by protein acyltransferase (PAT). In this study, an MdPAT family member, MdPAT16, was identified and shown to have palmitoyltransferase activity. We found that this gene responded to salt stress and that its expression improved plant salt resistance. MdPAT16 was shown to interact with MdCBL1 and stabilize MdCBL1 protein levels through palmitoylation. MdPAT16 further regulated apple sugar content by stabilizing the MdCIPK13-MdSUT2.2 protein complex. We found that the N-terminal sequence of MdCBL1 contains a palmitoylation site and that the N-terminal deletion of MdCBL1 leads to changes in protein stability and subcellular localization. Finally, exogenous salt stress increased the interaction of MdPAT16 with MdCBL1 and the sugar content in apple. These findings suggest that MdPAT16 functions as a stable means for the palmitoylation of downstream protein. It may be a missing link in the plant salt stress response pathway and have an important impact on fruit quality.