Phosphorylation of RACK1 in plants

Jin Gui Chen

doi:10.1080/15592324.2015.1022013

Phosphorylation of RACK1 in plants

Jin Gui Chen

Plant Systems Biology

Research output: Contribution to journal › Review article › peer-review

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 language	English
Journal	Plant Signaling and Behavior
Volume	10
Issue number	8
DOIs	https://doi.org/10.1080/15592324.2015.1022013
State	Published - 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.

Funders	Funder 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

Access to Document

10.1080/15592324.2015.1022013

Cite this

@article{260efaa02d63434cb77ef41ea7b1b34b,

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

keywords = "Arabidopsis, Kinase, Phosphorylation, Protein degradation, RACK1, Scaffold protein, WNK8",

author = "Chen, {Jin Gui}",

note = "Publisher Copyright: {\textcopyright} 2015 Taylor and Francis Group, LLC.",

year = "2015",

doi = "10.1080/15592324.2015.1022013",

language = "English",

volume = "10",

journal = "Plant Signaling and Behavior",

issn = "1559-2316",

publisher = "Taylor and Francis Group",

number = "8",

}

TY - JOUR

T1 - Phosphorylation of RACK1 in plants

AU - Chen, Jin Gui

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

KW - Arabidopsis

KW - Kinase

KW - Phosphorylation

KW - Protein degradation

KW - RACK1

KW - Scaffold protein

KW - WNK8

UR - http://www.scopus.com/inward/record.url?scp=84953776274&partnerID=8YFLogxK

U2 - 10.1080/15592324.2015.1022013

DO - 10.1080/15592324.2015.1022013

M3 - Review article

C2 - 26322575

AN - SCOPUS:84953776274

SN - 1559-2316

VL - 10

JO - Plant Signaling and Behavior

JF - Plant Signaling and Behavior

IS - 8

ER -

Phosphorylation of RACK1 in plants

Abstract

Funding

Keywords

Access to Document

Other files and links

Fingerprint

Cite this