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Signal integration by chloroplast phosphorylation networks: an update

Forty years after the initial discovery of light-dependent protein phosphorylation at the thylakoid membrane system, we are now beginning to understand the roles of chloroplast phosphorylation networks in their function to decode and mediate information on the metabolic status of the organelle to lo...

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Detalles Bibliográficos
Autores principales: Schönberg, Anna, Baginsky, Sacha
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3501822/
https://www.ncbi.nlm.nih.gov/pubmed/23181067
http://dx.doi.org/10.3389/fpls.2012.00256
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author Schönberg, Anna
Baginsky, Sacha
author_facet Schönberg, Anna
Baginsky, Sacha
author_sort Schönberg, Anna
collection PubMed
description Forty years after the initial discovery of light-dependent protein phosphorylation at the thylakoid membrane system, we are now beginning to understand the roles of chloroplast phosphorylation networks in their function to decode and mediate information on the metabolic status of the organelle to long-term adaptations in plastid and nuclear gene expression. With the help of genetics and functional genomics tools, chloroplast kinases and several hundred phosphoproteins were identified that now await detailed functional characterization. The regulation and the target protein spectrum of some kinases are understood, but this information is fragmentary with respect to kinase and target protein crosstalk in a changing environment. In this review, we will highlight the most recent advances in the field and discuss approaches that might lead to a comprehensive understanding of plastid signal integration by protein phosphorylation.
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spelling pubmed-35018222012-11-23 Signal integration by chloroplast phosphorylation networks: an update Schönberg, Anna Baginsky, Sacha Front Plant Sci Plant Science Forty years after the initial discovery of light-dependent protein phosphorylation at the thylakoid membrane system, we are now beginning to understand the roles of chloroplast phosphorylation networks in their function to decode and mediate information on the metabolic status of the organelle to long-term adaptations in plastid and nuclear gene expression. With the help of genetics and functional genomics tools, chloroplast kinases and several hundred phosphoproteins were identified that now await detailed functional characterization. The regulation and the target protein spectrum of some kinases are understood, but this information is fragmentary with respect to kinase and target protein crosstalk in a changing environment. In this review, we will highlight the most recent advances in the field and discuss approaches that might lead to a comprehensive understanding of plastid signal integration by protein phosphorylation. Frontiers Media S.A. 2012-11-20 /pmc/articles/PMC3501822/ /pubmed/23181067 http://dx.doi.org/10.3389/fpls.2012.00256 Text en Copyright © Schönberg and Baginsky. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/) , which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
spellingShingle Plant Science
Schönberg, Anna
Baginsky, Sacha
Signal integration by chloroplast phosphorylation networks: an update
title Signal integration by chloroplast phosphorylation networks: an update
title_full Signal integration by chloroplast phosphorylation networks: an update
title_fullStr Signal integration by chloroplast phosphorylation networks: an update
title_full_unstemmed Signal integration by chloroplast phosphorylation networks: an update
title_short Signal integration by chloroplast phosphorylation networks: an update
title_sort signal integration by chloroplast phosphorylation networks: an update
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3501822/
https://www.ncbi.nlm.nih.gov/pubmed/23181067
http://dx.doi.org/10.3389/fpls.2012.00256
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