Large-Scale Arabidopsis Phosphoproteome Profiling Reveals Novel Chloroplast Kinase Substrates and Phosphorylation Networks

DOI PDF 被引用文献12件
  • Sonja Reiland
    Department of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland (S.R., G.M., K.B., B.G., A.E., J.G., W.G., S.B.); Functional Genomics Center Zurich, 8057 Zurich, Switzerland (B.G., J.G.); and Institute of Plant Biology, University of Zurich, 8008 Zurich, Switzerland (A.E.)
  • Gaëlle Messerli
    Department of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland (S.R., G.M., K.B., B.G., A.E., J.G., W.G., S.B.); Functional Genomics Center Zurich, 8057 Zurich, Switzerland (B.G., J.G.); and Institute of Plant Biology, University of Zurich, 8008 Zurich, Switzerland (A.E.)
  • Katja Baerenfaller
    Department of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland (S.R., G.M., K.B., B.G., A.E., J.G., W.G., S.B.); Functional Genomics Center Zurich, 8057 Zurich, Switzerland (B.G., J.G.); and Institute of Plant Biology, University of Zurich, 8008 Zurich, Switzerland (A.E.)
  • Bertran Gerrits
    Department of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland (S.R., G.M., K.B., B.G., A.E., J.G., W.G., S.B.); Functional Genomics Center Zurich, 8057 Zurich, Switzerland (B.G., J.G.); and Institute of Plant Biology, University of Zurich, 8008 Zurich, Switzerland (A.E.)
  • Anne Endler
    Department of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland (S.R., G.M., K.B., B.G., A.E., J.G., W.G., S.B.); Functional Genomics Center Zurich, 8057 Zurich, Switzerland (B.G., J.G.); and Institute of Plant Biology, University of Zurich, 8008 Zurich, Switzerland (A.E.)
  • Jonas Grossmann
    Department of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland (S.R., G.M., K.B., B.G., A.E., J.G., W.G., S.B.); Functional Genomics Center Zurich, 8057 Zurich, Switzerland (B.G., J.G.); and Institute of Plant Biology, University of Zurich, 8008 Zurich, Switzerland (A.E.)
  • Wilhelm Gruissem
    Department of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland (S.R., G.M., K.B., B.G., A.E., J.G., W.G., S.B.); Functional Genomics Center Zurich, 8057 Zurich, Switzerland (B.G., J.G.); and Institute of Plant Biology, University of Zurich, 8008 Zurich, Switzerland (A.E.)
  • Sacha Baginsky
    Department of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland (S.R., G.M., K.B., B.G., A.E., J.G., W.G., S.B.); Functional Genomics Center Zurich, 8057 Zurich, Switzerland (B.G., J.G.); and Institute of Plant Biology, University of Zurich, 8008 Zurich, Switzerland (A.E.)

説明

<jats:title>Abstract</jats:title><jats:p>We have characterized the phosphoproteome of Arabidopsis (Arabidopsis thaliana) seedlings using high-accuracy mass spectrometry and report the identification of 1,429 phosphoproteins and 3,029 unique phosphopeptides. Among these, 174 proteins were chloroplast phosphoproteins. Motif-X (motif extractor) analysis of the phosphorylation sites in chloroplast proteins identified four significantly enriched kinase motifs, which include casein kinase II (CKII) and proline-directed kinase motifs, as well as two new motifs at the carboxyl terminus of ribosomal proteins. Using the phosphorylation motifs as a footprint for the activity of a specific kinase class, we connected the phosphoproteins with their putative kinases and constructed a chloroplast CKII phosphorylation network. The network topology suggests that CKII is a central regulator of different chloroplast functions. To provide insights into the dynamic regulation of protein phosphorylation, we analyzed the phosphoproteome at the end of day and end of night. The results revealed only minor changes in chloroplast kinase activities and phosphorylation site utilization. A notable exception was ATP synthase β-subunit, which is found phosphorylated at CKII phosphorylation sites preferentially in the dark. We propose that ATP synthase is regulated in cooperation with 14-3-3 proteins by CKII-mediated phosphorylation of ATP synthase β-subunit in the dark.</jats:p>

収録刊行物

  • Plant Physiology

    Plant Physiology 150 (2), 889-903, 2009-04-17

    Oxford University Press (OUP)

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