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Title: Phosphorylation of RACK1 in plants

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. In conclusion, these findings promote a new regulatory system in which the action of RACK1 is controlled by phosphorylation and subsequent protein degradation.

Authors:
 [1]
  1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE Office of Science (SC); USDOE Laboratory Directed Research and Development (LDRD) Program
OSTI Identifier:
1265401
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Plant Signaling & Behavior
Additional Journal Information:
Journal Volume: 10; Journal Issue: 8; Journal ID: ISSN 1559-2316
Publisher:
Taylor & Francis
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; arabidopsis; kinase; phosphorylation; protein degradation; RACK1; scaffold protein; WNK8

Citation Formats

Chen, Jay -Gui. Phosphorylation of RACK1 in plants. United States: N. p., 2015. Web. doi:10.1080/15592324.2015.1022013.
Chen, Jay -Gui. Phosphorylation of RACK1 in plants. United States. https://doi.org/10.1080/15592324.2015.1022013
Chen, Jay -Gui. Mon . "Phosphorylation of RACK1 in plants". United States. https://doi.org/10.1080/15592324.2015.1022013. https://www.osti.gov/servlets/purl/1265401.
@article{osti_1265401,
title = {Phosphorylation of RACK1 in plants},
author = {Chen, Jay -Gui},
abstractNote = {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. In conclusion, these findings promote a new regulatory system in which the action of RACK1 is controlled by phosphorylation and subsequent protein degradation.},
doi = {10.1080/15592324.2015.1022013},
journal = {Plant Signaling & Behavior},
number = 8,
volume = 10,
place = {United States},
year = {Mon Aug 31 00:00:00 EDT 2015},
month = {Mon Aug 31 00:00:00 EDT 2015}
}

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Cited by: 7 works
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Works referencing / citing this record:

Molecular Features and mRNA Expression of the Receptor for Activated C Kinase 1 from Symbiodinium microadriaticum ssp. microadriaticum During Growth and the Light/Dark cycle
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Broad Substrate-Specific Phosphorylation Events Are Associated With the Initial Stage of Plant Cell Wall Recognition in Neurospora crassa
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Proteomic Analysis of Rapeseed Root Response to Waterlogging Stress
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