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2016 MBAS Admission Announcement (early-decision deadline: 1/31, final deadline: 3/31) 01/20/2016
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Hsing-Yi Cho, Tuan-Nan Wen, Ying-Tsui Wang and Ming-Che Shih* (2016) Quantitative Phosphoproteomics of Protein Kinase SnRK1 regulated protein phosphorylation in Arabidopsis under Submergence - Journal of Experimental Botany. 67(9): 2745-60.

SNF1 RELATED PROTEIN KINASE 1 (SnRK1) is proposed to be a central integrator of plant stress and energy starvation signaling pathways. We observed in this study that the Arabidopsis SnRK1.1 dominant negative mutant (SnRK1.1K48M) had lower tolerance to submergence than the wild-type, suggesting that SnRK1.1-dependent phosphorylation of target proteins is important in signaling pathways triggered by submergence. We conducted quantitative phosphoproteomics and found that the phosphorylation levels of 57 proteins increased and the levels of 27 proteins decreased in Col-0 within 0.5–3 h of submergence. Among the 57 proteins with increased phosphorylation in Col-0, 38 did not show increased phosphorylation levels in SnRK1.1K48M under submergence. These proteins are involved mainly in sugar and protein synthesis. In particular, the phosphorylation of MPK6, which is involved in regulating ROS responses under abiotic stresses, was disrupted in the SnRK1.1K48M mutant. In addition, PTP1, a negative regulator of MPK6 activity that directly dephosphorylates MPK6, was also regulated by SnRK1.1. We further showed that the energy conservation was disrupted in SnRK1.1K48M, mpk6 and PTP1S7AS8A under submergence. These results reveal insights into the function of SnRK1 and the downstream signaling factors related to submergence.




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