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Mol Plant. 2009 Nov;2(6):1141-53. doi: 10.1093/mp/ssp058. Epub 2009 Aug 10.

The chloroplast kinase network: new insights from large-scale phosphoproteome profiling.

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1
Department of Biology, ETH Zurich, Universit├Ątstrasse 2, 8092 Z├╝rich, Switzerland. sbaginsky@ethz.ch

Abstract

Protein phosphorylation is one of the most important posttranslational modifications in eukaryotic cells and affects almost all basic cellular processes. The chloroplast as plant-specific cell organelle with important metabolic functions is integrated into the cellular signaling and phosphorylation network. Recent large-scale chloroplast phosphoproteome analyses in Arabidopsis have provided new information about phosphorylation targets and expanded the list of chloroplast metabolic and regulatory functions that are potentially controlled by protein phosphorylation. Phosphorylated peptides identified from chloroplast proteins provide new insights into phosphorylation motifs, protein kinase activities, and substrate utilization. Phosphorylation sites in protein kinases can reveal chloroplast phosphorylation cascades that may network different functions by integrating signaling chains. Our review provides a meta-analysis of currently available chloroplast phosphoproteome information and discusses biological insights from large-scale chloroplast phosphoprotein profiling as well as technological constraints of kinase network analysis.

PMID:
19995723
DOI:
10.1093/mp/ssp058
[Indexed for MEDLINE]
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