The phosphorylation state of chloroplast transit peptides regulates preprotein import

Lamberti, G., Drurey, C. , Soll, J. and Schwenkert, S. (2011) The phosphorylation state of chloroplast transit peptides regulates preprotein import. Plant Signaling and Behavior, 6(12), pp. 1918-1920. (doi: 10.4161/psb.6.12.18127) (PMID:22105029) (PMCID:PMC3337178)

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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.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Drurey, Claire
Authors: Lamberti, G., Drurey, C., Soll, J., and Schwenkert, S.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Plant Signaling and Behavior
Publisher:Taylor & Francis
ISSN (Online):1559-2324
Published Online:01 December 2011

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