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Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 21))

Summary

Application of novel techniques for the characterization of in vivo protein phosphorylation has revealed sixteen distinct phosphorylation sites in ten integral and two peripheral proteins in photosynthetic thylakoid membranes. In addition to phosphorylation of the photosystem II (PS II) proteins D1, D2, CP43, and PsbH, and the light-harvesting antenna polypeptides LHCII and CP29, phosphorylation has been found in photosystem I (PS I) protein PsaD and in two recently identified proteins TSP9 and TMP14. The accumulated knowledge favors an involvement of reversible phosphorylation in adaptive stress responses and cellular signaling, but not in direct regulation of photosynthetic activities like electron transfer or oxygen evolution. Enhancement of PS II protein phosphorylation by abiotic stress maintains the integrity of PS II before it migrates to the stroma regions of the thylakoids where dephosphorylation and subsequent protein turnover take place. Specific dephosphorylation of the D1, D2, and CP43 polypeptides is performed by a heat shock-inducible protein phosphatase intrinsic to the thylakoid membrane. The phosphatase activity is regulated by the lumenal peptidyl-prolyl isomerase TLP40. This regulation may coordinate the protein folding activity of TLP40 in the lumen with the protein dephosphorylation at the opposite side of the thylakoid membrane. Reversible phosphorylation of LHCII in vivo is under complex redox and metabolic control and is probably involved in regulation of the size of the PS II antennae. Cold- and high light-induced phosphorylation of CP29 may facilitate photoprotective energy dissipation by changing PS II-LHCII interactions under stress conditions. Phosphorylation of PsaD protein could be involved in regulation of PS I stability and ferredoxin reduction by PS I. The light-induced phosphorylation of TSP9, followed by its release from thylakoids, is implicated in plant cell signaling. The exact physiological roles of the protein phosphorylation events in thylakoids should be revealed by studies with appropriate mutants of plants and algae

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Vener, A.V. (2008). Phosphorylation of Thylakoid Proteins. In: Demmig-Adams, B., Adams, W.W., Mattoo, A.K. (eds) Photoprotection, Photoinhibition, Gene Regulation, and Environment. Advances in Photosynthesis and Respiration, vol 21. Springer, Dordrecht. https://doi.org/10.1007/1-4020-3579-9_8

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