Lamberti 2011 Plant Signal Behav: Difference between revisions
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{{Publication | {{Publication | ||
|title=Lamberti G, Drurey C, Soll J, Schwenkert S (2011) The phosphorylation state of chloroplast transit peptides regulates preprotein import. Plant Signal Behav 6 | |title=Lamberti G, Drurey C, Soll J, Schwenkert S (2011) The phosphorylation state of chloroplast transit peptides regulates preprotein import. Plant Signal Behav 6:1918-20. | ||
|info=http://www.ncbi.nlm.nih.gov/pubmed/22105029 | |info=[http://www.ncbi.nlm.nih.gov/pubmed/22105029 PMID: 22105029] | ||
|authors=Lamberti G, Drurey C, Soll J, Schwenkert S | |authors=Lamberti G, Drurey C, Soll J, Schwenkert S | ||
|year=2011 | |year=2011 | ||
|journal=Plant Signal Behav | |journal=Plant Signal Behav | ||
|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 | |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. | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
| | |organism=Plants | ||
|preparations=Chloroplasts | |preparations=Chloroplasts | ||
}} | }} |
Latest revision as of 10:15, 9 November 2016
Lamberti G, Drurey C, Soll J, Schwenkert S (2011) The phosphorylation state of chloroplast transit peptides regulates preprotein import. Plant Signal Behav 6:1918-20. |
Lamberti G, Drurey C, Soll J, Schwenkert S (2011) Plant Signal Behav
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.
Labels:
Organism: Plants
Preparation: Chloroplasts