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Title of Journal: Plant Mol Biol Rep

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Abbravation: Plant Molecular Biology Reporter

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Springer US

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DOI

10.1002/jccs.200200071

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1572-9818

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Differential Protein Phosphorylation Regulates Chl

Authors: Edouard BoexFontvieille Mathieu Jossier Marlène Davanture Michel Zivy Michael Hodges Guillaume Tcherkez
Publish Date: 2014/02/27
Volume: 32, Issue: 5, Pages: 987-1001
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Abstract

Phototropindependent chloroplast movement is essential to the photosynthetic acclimation of mesophyll cells to incident light Chloroplast movement involves many cellular actors such as chloroplastassociated actin filaments and proteins that mediate signalling between phototropins and chloroplast motion In the past few years genetic approaches have identified several key proteins but the intrinsic mechanisms of the signalling cascade such as phosphorylation events remain undefined Here we took advantage of phosphoproteomics to examine the involvement of protein phosphorylation in chloroplast movement in darkness or under high light at different CO2 mole fractions 100 380 or 1000 ppm to vary photosynthetic activity Amongst the 100 relevant identified phosphopeptides 19 corresponding to 8 proteins were differentially phosphorylated in darkness vs high light There was no significant CO2 effect on the observed phosphorylation patterns We further characterized the phosphorylation sites in THRUMIN1 which is believed to be crucial for the attachment of chloroplastassociated actin filaments to the plasma membrane and thus for chloroplast movements The mutant thrumin1 was complemented with a mutated protein in which phosphosites were substituted to a phosphomimetic Asp or a nonphosphorylatable Ala residue While the phosphomimetic substitution altered the chloroplast response in the light only both light and dark responses were altered with the nonphosphorylatable substitution Our data suggest a key role of protein phosphorylation including that of THRUMIN1 in the light/dark control of chloroplast movementsThis work was supported by the Institut Fédératif de Recherche 87 for the phosphoproteomics analyses and the Agence Nationale de la Recherche for running costs 2 Jeunes Chercheurs grants to GT under contract nos 08–330055 and 12–000101 E BF was supported by the Labex Saclay Plant Science through a postdoctoral grant

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