title: The phosphorylation state of chloroplast transit peptides regulates preprotein import.
abstract: Import of nuclear encoded proteins into chloroplast is an essential and well-regulated mechanism. The cytosolic kinases STY8, STY17 and STY46 have been shown to phosphorylate chloroplast preprotein transit peptides advantaging the binding of a 14-3-3 dimer. Analyses of sty8 sty17 sty46 mutant plants revealed a role for the kinases in chloroplast differentiation, possibly due to lack of transit peptide phosphorylation. Moreover we could show that not only phosphorylation but also transit peptide dephosphorylation appears to be required for the fine regulation of the back-transport of nuclear encoded proteins to the chloroplast.
authors: Department of Biology I, Botany, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
authors: Giorgia
authors: G
authors: Lamberti
authors: Claire
authors: C
authors: Drurey
authors: Jürgen
authors: J
authors: Soll
authors: Serena
authors: S
authors: Schwenkert
mesh_terms: D017360:Arabidopsis / Q000378:metabolism; D060365:Chloroplast Proteins / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism; D010766:Phosphorylation; D010940:Plant Proteins / Q000378:metabolism*; D021382:Protein Sorting Signals; D021381:Protein Transport
chemical_list: D060365:Chloroplast Proteins; D010940:Plant Proteins; D021382:Protein Sorting Signals; C078737:chloroplast transit peptides