Document Detail

Protein kinases and phosphatases involved in the acclimation of the photosynthetic apparatus to a changing light environment.
MedLine Citation:
PMID:  23148273     Owner:  NLM     Status:  MEDLINE    
Photosynthetic organisms are subjected to frequent changes in light quality and quantity and need to respond accordingly. These acclimatory processes are mediated to a large extent through thylakoid protein phosphorylation. Recently, two major thylakoid protein kinases have been identified and characterized. The Stt7/STN7 kinase is mainly involved in the phosphorylation of the LHCII antenna proteins and is required for state transitions. It is firmly associated with the cytochrome b(6)f complex, and its activity is regulated by the redox state of the plastoquinone pool. The other kinase, Stl1/STN8, is responsible for the phosphorylation of the PSII core proteins. Using a reverse genetics approach, we have recently identified the chloroplast PPH1/TAP38 and PBPC protein phosphatases, which counteract the activity of STN7 and STN8 kinases, respectively. They belong to the PP2C-type phosphatase family and are conserved in land plants and algae. The picture that emerges from these studies is that of a complex regulatory network of chloroplast protein kinases and phosphatases that is involved in light acclimation, in maintenance of the plastoquinone redox poise under fluctuating light and in the adjustment to metabolic needs.
Jean-David Rochaix; Sylvain Lemeille; Alexey Shapiguzov; Iga Samol; Geoffrey Fucile; Adrian Willig; Michel Goldschmidt-Clermont
Related Documents :
21170023 - The assembly of a gtpase-kinase signalling complex by a bacterial catalytic scaffold.
2359593 - Disaturated phosphatidylcholine in rabbit eustachian tube surfactant.
11753643 - Novel cross talk between mek and s6k2 in fgf-2 induced proliferation of sclc cells.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Philosophical transactions of the Royal Society of London. Series B, Biological sciences     Volume:  367     ISSN:  1471-2970     ISO Abbreviation:  Philos. Trans. R. Soc. Lond., B, Biol. Sci.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-11-13     Completed Date:  2013-04-22     Revised Date:  2014-01-10    
Medline Journal Info:
Nlm Unique ID:  7503623     Medline TA:  Philos Trans R Soc Lond B Biol Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  3466-74     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Sequence
Arabidopsis / enzymology*,  genetics,  radiation effects
Arabidopsis Proteins / genetics,  metabolism*
Chlamydomonas reinhardtii / enzymology,  genetics
Chloroplasts / enzymology,  genetics
Light-Harvesting Protein Complexes / genetics,  metabolism
Molecular Sequence Data
Phosphoprotein Phosphatases / genetics,  metabolism*
Photosystem II Protein Complex / genetics,  metabolism
Plastoquinone / metabolism
Protein Kinases / genetics,  metabolism*
Protein-Serine-Threonine Kinases / genetics,  metabolism*
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Light-Harvesting Protein Complexes; 0/Photosystem II Protein Complex; EC 2.7.-/Protein Kinases; EC Kinases; EC protein, Arabidopsis; EC protein, Arabidopsis; EC Phosphatases; EC protein, Arabidopsis; OAC30J69CN/Plastoquinone

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Optimization of light harvesting and photoprotection: molecular mechanisms and physiological consequ...
Next Document:  Redox regulation of photosynthetic gene expression.