Phosphorylation of RACK1 in plants

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10 Scopus citations

Abstract

Receptor for Activated C Kinase 1 (RACK1) is a versatile scaffold protein that interacts with a large, diverse group of proteins to regulate various signaling cascades. RACK1 has been shown to regulate hormonal signaling, stress responses and multiple processes of growth and development in plants. However, little is known about the molecular mechanism underlying these regulations. Recently, it has been demonstrated that Arabidopsis RACK1 is phosphorylated by an atypical serine/threonine protein kinase, WITH NO LYSINE 8 (WNK8). Furthermore, RACK1 phosphorylation by WNK8 negatively regulates RACK1 function by influencing its protein stability. These findings promote a new regulatory system in which the action of RACK1 is controlled by phosphorylation and subsequent protein degradation.

Original languageEnglish
JournalPlant Signaling and Behavior
Volume10
Issue number8
DOIs
StatePublished - 2015

Funding

This work was supported by the Plant-Microbe Interfaces Scientific Focus Area in the Genomic Science Program, United States Department of Energy, Office of Science, Biological and Environmental Research. Oak Ridge National Laboratory is managed by UT-Battelle, LLC, for the United States Department of Energy under contract DE-AC05–00OR22725.

FundersFunder number
Plant-Microbe Interfaces Scientific Focus Area
United States Department of Energy
Office of Science
Biological and Environmental Research

    Keywords

    • Arabidopsis
    • Kinase
    • Phosphorylation
    • Protein degradation
    • RACK1
    • Scaffold protein
    • WNK8

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