TY - JOUR
T1 - Quantitative proteomics and phosphoproteomics support a role for mut9-like kinases in multiple metabolic and signaling pathways in Arabidopsis
AU - Wilson, Margaret E.
AU - Tzeng, Shin Cheng
AU - Augustin, Megan M.
AU - Meyer, Matthew
AU - Jiang, Xiaoyue
AU - Choi, Jae H.
AU - Rogers, John C.
AU - Evans, Bradley S.
AU - Kutchan, Toni M.
AU - Nusinow, Dmitri A.
N1 - Funding Information:
Acknowledgments—This material is based upon work supported by the National Science Foundation under Grant No. DBI-1827534 for acquisition of the Orbitrap Fusion Lumos LC-MS/MS. The authors thank Maria L. Sorkin, He Huang, and Rebecca Bindbeutel for helpful comments in the preparation of the manuscript.
Publisher Copyright:
© 2021 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
PY - 2021
Y1 - 2021
N2 - Protein phosphorylation is one of the most prevalent posttranslational modifications found in eukaryotic systems. It serves as a key molecular mechanism that regulates protein function in response to environmental stimuli. The Mut9-like kinases (MLKs) are a plant-specific family of Ser/Thr kinases linked to light, circadian, and abiotic stress signaling. Here we use quantitative phosphoproteomics in conjunction with global proteomic analysis to explore the role of the MLKs in daily protein dynamics. Proteins involved in light, circadian, and hormone signaling, as well as several chromatin-modifying enzymes and DNA damage response factors, were found to have altered phosphorylation profiles in the absence of MLK family kinases. In addition to altered phosphorylation levels, mlk mutant seedlings have an increase in glucosinolate metabolism enzymes. Subsequently, we show that a functional consequence of the changes to the proteome and phosphoproteome in mlk mutant plants is elevated glucosinolate accumulation and increased sensitivity to DNA damaging agents. Combined with previous reports, this work supports the involvement of MLKs in a diverse set of stress responses and developmental processes, suggesting that the MLKs serve as key regulators linking environmental inputs to developmental outputs.
AB - Protein phosphorylation is one of the most prevalent posttranslational modifications found in eukaryotic systems. It serves as a key molecular mechanism that regulates protein function in response to environmental stimuli. The Mut9-like kinases (MLKs) are a plant-specific family of Ser/Thr kinases linked to light, circadian, and abiotic stress signaling. Here we use quantitative phosphoproteomics in conjunction with global proteomic analysis to explore the role of the MLKs in daily protein dynamics. Proteins involved in light, circadian, and hormone signaling, as well as several chromatin-modifying enzymes and DNA damage response factors, were found to have altered phosphorylation profiles in the absence of MLK family kinases. In addition to altered phosphorylation levels, mlk mutant seedlings have an increase in glucosinolate metabolism enzymes. Subsequently, we show that a functional consequence of the changes to the proteome and phosphoproteome in mlk mutant plants is elevated glucosinolate accumulation and increased sensitivity to DNA damaging agents. Combined with previous reports, this work supports the involvement of MLKs in a diverse set of stress responses and developmental processes, suggesting that the MLKs serve as key regulators linking environmental inputs to developmental outputs.
UR - http://www.scopus.com/inward/record.url?scp=85105311986&partnerID=8YFLogxK
U2 - 10.1016/J.MCPRO.2021.100063
DO - 10.1016/J.MCPRO.2021.100063
M3 - Article
C2 - 33677124
AN - SCOPUS:85105311986
SN - 1535-9476
VL - 20
JO - Molecular and Cellular Proteomics
JF - Molecular and Cellular Proteomics
M1 - 100063
ER -