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@ARTICLE{Uhrig:888485,
      author       = {Uhrig, R. Glen and Echevarría-Zomeño, Sira and Schlapfer,
                      Pascal and Grossmann, Jonas and Roschitzki, Bernd and
                      Koerber, Niklas and Fiorani, Fabio and Gruissem, Wilhelm},
      title        = {{D}iurnal {D}ynamics of the {A}rabidopsis {R}osette
                      {P}roteome and {P}hosphoproteome},
      journal      = {Plant, cell $\&$ environment},
      volume       = {44},
      number       = {3},
      issn         = {1365-3040},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2020-04949},
      pages        = {821-841},
      year         = {2021},
      abstract     = {Plant growth depends on the diurnal regulation of cellular
                      processes, but it is not well understood if and how
                      transcriptional regulation controls diurnal fluctuations at
                      the protein‐level. Here we report a high‐resolution
                      Arabidopsis thaliana (Arabidopsis) leaf rosette proteome
                      acquired over a 12 h light : 12 h dark diurnal cycle and the
                      phosphoproteome immediately before and after the
                      light‐to‐dark and dark‐to‐light transitions. We
                      quantified nearly 5000 proteins and 800 phosphoproteins, of
                      which 288 fluctuated in their abundance and 226 fluctuated
                      in their phosphorylation status. Of the phosphoproteins,
                      $60\%$ were quantified for changes in protein abundance.
                      This revealed six proteins involved in nitrogen and hormone
                      metabolism that had concurrent changes in both protein
                      abundance and phosphorylation status. The diurnal proteome
                      and phosphoproteome changes involve proteins in key cellular
                      processes, including protein translation, light perception,
                      photosynthesis, metabolism and transport. The
                      phosphoproteome at the light‐dark transitions revealed the
                      dynamics at phosphorylation sites in either anticipation of
                      or response to a change in light regime. Phosphorylation
                      site motif analyses implicate casein kinase II and
                      calcium/calmodulin dependent kinases among the primary
                      light‐dark transition kinases. The comparative analysis of
                      the diurnal proteome and diurnal and circadian transcriptome
                      established how mRNA and protein accumulation intersect in
                      leaves during the diurnal cycle of the plant.},
      cin          = {IBG-2},
      ddc          = {580},
      cid          = {I:(DE-Juel1)IBG-2-20101118},
      pnm          = {582 - Plant Science (POF3-582) / 2171 - Biological and
                      environmental resources for sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF3-582 / G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33278033},
      UT           = {WOS:000603042100001},
      doi          = {10.1111/pce.13969},
      url          = {https://juser.fz-juelich.de/record/888485},
}