ArticlePlant physiology2015
Arabidopsis receptor of activated C kinase1 phosphorylation by WITH NO LYSINE8 KINASE.
Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 47 citations in OpenAlex.
- Identification of WNK Gene inPlants (Basel, Switzerland) · 2026Article
- Plant PAQR-like sensors activate heterotrimeric G proteins to confer resistance against multiple pathogens.Molecular plant · 2025Article
- Genome-wide identification and expression analysis of the WNK kinase gene family in soybean.Molecular breeding : new strategies in plant improvement · 2024Article
- Genome-Wide Identification and Analysis of the WNK Kinase Gene Family in Upland Cotton.Plants (Basel, Switzerland) · 2023Article
- Nuclear Localization of G3BP6 Is Essential for the Flowering Transition inBiomolecules · 2023Article
- Receptor for Activated C Kinase1B (RACK1B) Delays Salinity-Induced Senescence in Rice Leaves by Regulating Chlorophyll Degradation.Plants (Basel, Switzerland) · 2023Article
- Article
- With no lysine kinases: the key regulatory networks and phytohormone cross talk in plant growth, development and stress response.Plant cell reports · 2021Review
- Upstream Open Reading Frame Mediated Translation of WNK8 Is Required for ABA Response inInternational journal of molecular sciences · 2021Article
- Selective regulation in ribosome biogenesis and protein production for efficient viral translation.Archives of microbiology · 2021Review
- Broad Substrate-Specific Phosphorylation Events Are Associated With the Initial Stage of Plant Cell Wall Recognition inFrontiers in microbiology · 2019Article
- OsRACK1A, encodes a circadian clock-regulated WD40 protein, negatively affect salt tolerance in rice.Rice (New York, N.Y.) · 2018Article
- Alteration of cell wall xylan acetylation triggers defense responses that counterbalance the immune deficiencies of plants impaired in the β-subunit of the heterotrimeric G-protein.The Plant journal : for cell and molecular biology · 2017Article
- Sumoylation stabilizes RACK1B and enhance its interaction with RAP2.6 in the abscisic acid response.Scientific reports · 2017Article
- Asc1p/RACK1 Connects Ribosomes to Eukaryotic Phosphosignaling.Molecular and cellular biology · 2017Article
- Tyrosine Phosphorylation Based Homo-dimerization of Arabidopsis RACK1A Proteins Regulates Oxidative Stress Signaling Pathways in Yeast.Frontiers in plant science · 2016Article
- The Receptor for Activated C Kinase in Plant Signaling: Tale of a Promiscuous Little Molecule.Frontiers in plant science · 2015Review
- Phosphorylation of RACK1 in plants.Plant signaling & behavior · 2015Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
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. Here, 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, RACK1A(S122A/T162A), but not the phosphomimetic form, RACK1A(S122D/T162E), rescued the rack1a null mutant, implying that phosphorylation at Ser-122 and Thr-162 negatively regulates RACK1A function. The transcript of RACK1A(S122D/T162E) accumulated at similar levels as those of RACK1(S122A/T162A). However, although the steady-state level of the RACK1A(S122A/T162A) protein was similar to wild-type RACK1A protein, the RACK1A(S122D/T162E) protein was nearly undetectable, suggesting that phosphorylation affects the stability of RACK1A proteins. Taken together, these results suggest that RACK1 is phosphorylated by WNK8 and that phosphorylation negatively regulates RACK1 function by influencing its protein stability.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.