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The calcium‐dependent protein kinase CPK7 acts on root hydraulic conductivity
Authors:GUOWEI LI  MARIE BOUDSOCQ  SONIA HEM  JÉRÔME VIALARET  MICHEL ROSSIGNOL  CHRISTOPHE MAUREL  VÉRONIQUE SANTONI
Institution:1. Biochimie et Physiologie Moléculaire des Plantes, INRA/CNRS/SupAgro/UM2, UMR 5004, Montpellier Cedex 1, France;2. Saclay Plant Sciences, Institut des Sciences du Végétal, Gif‐sur‐Yvette Cedex, France;3. Laboratoire de Protéomique Fonctionnelle, Montpellier Cedex 1, France
Abstract:The hydraulic conductivity of plant roots (Lpr) is determined in large part by the activity of aquaporins. Mechanisms occurring at the post‐translational level, in particular phosphorylation of aquaporins of the plasma membrane intrinsic protein 2 (PIP2) subfamily, are thought to be of critical importance for regulating root water transport. However, knowledge of protein kinases and phosphatases acting on aquaporin function is still scarce. In the present work, we investigated the Lpr of knockout Arabidopsis plants for four Ca2+‐dependent protein kinases. cpk7 plants showed a 30% increase in Lpr because of a higher aquaporin activity. A quantitative proteomic analysis of wild‐type and cpk7 plants revealed that PIP gene expression and PIP protein quantity were not correlated and that CPK7 has no effect on PIP2 phosphorylation. In contrast, CPK7 exerts a negative control on the cellular abundance of PIP1s, which likely accounts for the higher Lpr of cpk7. In addition, this study revealed that the cellular amount of a few additional proteins including membrane transporters is controlled by CPK7. The overall work provides evidence for CPK7‐dependent stability of specific membrane proteins.
Keywords:aquaporin  CDPK  phosphorylation  PIP  quantitative proteomics  root water transport
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