Arabidopsis Receptor of Activated C Kinase1 Phosphorylation by WITH NO LYSINE8 KINASE

Urano, Daisuke; Czarnecki, Olaf; Wang, Xiaoping; Jones, Alan M.; Chen, Jin-Gui

doi:10.1104/pp.114.247460

Title: Arabidopsis Receptor of Activated C Kinase1 Phosphorylation by WITH NO LYSINE8 KINASE

Abstract

Receptor of activated C kinase1 (RACK1) is a versatile scaffold protein that binds to numerous proteins to regulate diverse cellular pathways in mammals. In Arabidopsis (Arabidopsis thaliana), RACK1 has been shown to regulate plant hormone signaling, stress responses, and multiple processes of growth and development. However, little is known about the molecular mechanism underlying these regulations. In this paper, we show that an atypical serine (Ser)/threonine (Thr) protein kinase, WITH NO LYSINE8 (WNK8), phosphorylates RACK1. WNK8 physically interacted with and phosphorylated RACK1 proteins at two residues: Ser-122 and Thr-162. Genetic epistasis analysis of rack1 wnk8 double mutants indicated that RACK1 acts downstream of WNK8 in the glucose responsiveness and flowering pathways. The phosphorylation-dead form, RACK1AS122A/T162A, but not the phosphomimetic form, RACK1AS122D/T162E, rescued the rack1a null mutant, implying that phosphorylation at Ser-122 and Thr-162 negatively regulates RACK1A function. The transcript of RACK1AS122D/T162E accumulated at similar levels as those of RACK1S122A/T162A. However, although the steady-state level of the RACK1AS122A/T162A protein was similar to wild-type RACK1A protein, the RACK1AS122D/T162E protein was nearly undetectable, suggesting that phosphorylation affects the stability of RACK1A proteins. In conclusion, these results suggest that RACK1 is phosphorylated by WNK8 and that phosphorylation negatively regulates RACK1 function by influencing itsmore » protein stability.« less

Authors:

Urano, Daisuke ^[1]; Czarnecki, Olaf ^[2]; Wang, Xiaoping ^[3]; Jones, Alan M. ^[1]; Chen, Jin-Gui ^[2]

Univ. of North Carolina, Chapel Hill, NC (United States)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Northeast Normal University, Changchun (China)

Publication Date:: Mon Dec 08 00:00:00 EST 2014

Research Org.:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Org.:: USDOE Laboratory Directed Research and Development (LDRD) Program

OSTI Identifier:: 1286841

Grant/Contract Number:: AC05-00OR22725

Resource Type:: Accepted Manuscript

Journal Name:: Plant Physiology

Additional Journal Information:: Journal Volume: 167; Journal Issue: 2; Journal ID: ISSN 1532-2548

Publisher:: American Society of Plant Biologists

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES

Citation Formats


                    Urano, Daisuke, Czarnecki, Olaf, Wang, Xiaoping, Jones, Alan M., and Chen, Jin-Gui. Arabidopsis Receptor of Activated C Kinase1 Phosphorylation by WITH NO LYSINE8 KINASE.  United States: N. p., 2014. 
Web.  doi:10.1104/pp.114.247460.

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                    Urano, Daisuke, Czarnecki, Olaf, Wang, Xiaoping, Jones, Alan M., & Chen, Jin-Gui. Arabidopsis Receptor of Activated C Kinase1 Phosphorylation by WITH NO LYSINE8 KINASE.  United States.  https://doi.org/10.1104/pp.114.247460

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                    Urano, Daisuke, Czarnecki, Olaf, Wang, Xiaoping, Jones, Alan M., and Chen, Jin-Gui. Mon .  
"Arabidopsis Receptor of Activated C Kinase1 Phosphorylation by WITH NO LYSINE8 KINASE".  United States.  https://doi.org/10.1104/pp.114.247460.  https://www.osti.gov/servlets/purl/1286841.

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@article{osti_1286841,

  title        = {Arabidopsis Receptor of Activated C Kinase1 Phosphorylation by WITH NO LYSINE8 KINASE},

  author       = {Urano, Daisuke and Czarnecki, Olaf and Wang, Xiaoping and Jones, Alan M. and Chen, Jin-Gui},

  abstractNote = {Receptor of activated C kinase1 (RACK1) is a versatile scaffold protein that binds to numerous proteins to regulate diverse cellular pathways in mammals. In Arabidopsis (Arabidopsis thaliana), RACK1 has been shown to regulate plant hormone signaling, stress responses, and multiple processes of growth and development. However, little is known about the molecular mechanism underlying these regulations. In this paper, we show that an atypical serine (Ser)/threonine (Thr) protein kinase, WITH NO LYSINE8 (WNK8), phosphorylates RACK1. WNK8 physically interacted with and phosphorylated RACK1 proteins at two residues: Ser-122 and Thr-162. Genetic epistasis analysis of rack1 wnk8 double mutants indicated that RACK1 acts downstream of WNK8 in the glucose responsiveness and flowering pathways. The phosphorylation-dead form, RACK1AS122A/T162A, but not the phosphomimetic form, RACK1AS122D/T162E, rescued the rack1a null mutant, implying that phosphorylation at Ser-122 and Thr-162 negatively regulates RACK1A function. The transcript of RACK1AS122D/T162E accumulated at similar levels as those of RACK1S122A/T162A. However, although the steady-state level of the RACK1AS122A/T162A protein was similar to wild-type RACK1A protein, the RACK1AS122D/T162E protein was nearly undetectable, suggesting that phosphorylation affects the stability of RACK1A proteins. In conclusion, these results suggest that RACK1 is phosphorylated by WNK8 and that phosphorylation negatively regulates RACK1 function by influencing its protein stability.},

  doi          = {10.1104/pp.114.247460},

  journal      = {Plant Physiology},

  number       = 2,

  volume       = 167,

  place        = {United States},

  year         = {Mon Dec 08 00:00:00 EST 2014},

  month        = {Mon Dec 08 00:00:00 EST 2014}

}

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Works referencing / citing this record:

OsRACK1A, encodes a circadian clock-regulated WD40 protein, negatively affect salt tolerance in rice
journal, August 2018

Zhang, Dongping; Wang, Yuzhu; Shen, Jinyu
Rice, Vol. 11, Issue 1
DOI: 10.1186/s12284-018-0232-3

Broad Substrate-Specific Phosphorylation Events Are Associated With the Initial Stage of Plant Cell Wall Recognition in Neurospora crassa
journal, November 2019

Horta, Maria Augusta C.; Thieme, Nils; Gao, Yuqian
Frontiers in Microbiology, Vol. 10
DOI: 10.3389/fmicb.2019.02317

The Receptor for Activated C Kinase in Plant Signaling: Tale of a Promiscuous Little Molecule
journal, December 2015

Islas-Flores, Tania; Rahman, Ahasanur; Ullah, Hemayet
Frontiers in Plant Science, Vol. 6
DOI: 10.3389/fpls.2015.01090

Sumoylation stabilizes RACK1B and enhance its interaction with RAP2.6 in the abscisic acid response
journal, March 2017

Guo, Rongkai; Sun, Weining
Scientific Reports, Vol. 7, Issue 1
DOI: 10.1038/srep44090

OsRACK1A, encodes a circadian clock-regulated WD40 protein, negatively affect salt tolerance in rice
journal, August 2018

Zhang, Dongping; Wang, Yuzhu; Shen, Jinyu
Rice, Vol. 11, Issue 1
DOI: 10.1186/s12284-018-0232-3

The Receptor for Activated C Kinase in Plant Signaling: Tale of a Promiscuous Little Molecule
journal, December 2015

Islas-Flores, Tania; Rahman, Ahasanur; Ullah, Hemayet
Frontiers in Plant Science, Vol. 6
DOI: 10.3389/fpls.2015.01090

Tyrosine Phosphorylation Based Homo-dimerization of Arabidopsis RACK1A Proteins Regulates Oxidative Stress Signaling Pathways in Yeast
journal, February 2016

Sabila, Mercy; Kundu, Nabanita; Smalls, Deana
Frontiers in Plant Science, Vol. 7
DOI: 10.3389/fpls.2016.00176

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Similar Records

Title: Arabidopsis Receptor of Activated C Kinase1 Phosphorylation by WITH NO LYSINE8 KINASE

Abstract

Citation Formats

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