An autophosphorylation site database for leucine‐rich repeat receptor‐like kinases in <i><scp>A</scp>rabidopsis thaliana</i>

Mitra, Srijeet K.; Chen, Ruiqiang; Dhandaydham, Murali; Blackburn, R. Kevin; Kota, Uma; Goshe, Michael B.; Schwartz, Daniel; Clouse, Steven D.

doi:10.1111/tpj.12863

Cited by 36 publications

(37 citation statements)

References 62 publications

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“…Similarly, alignment of the EMS1-CD with its most related LRR-RLKs (BRI1, BRL1, BRL2, and BRL3) shows that only the Ser-892, Thr-914, and Ser-1076 phosphorylation sites are conserved, but nine other phosphorylation sites are diverse (Supplemental Fig. S7; Wang et al, 2005Wang et al, , 2008Mitra et al, 2015). Our studies showed that the S1076A mutation reduced 65% of EMS1 autophosphorylation activity.…”

Section: Discussionsupporting

confidence: 51%

“…Furthermore, among 24 in vitro-identified phosphorylation sites in SERK1, only three sites are due to bacterial transphosphorylation (Karlova et al, 2009). A recent study reported the identification of in vitro autophosphorylation sites in 73 LRR-RLKs, including SERK1 but not EMS1 (Mitra et al, 2015). In this study, we identified five in vitro Ser and Thr phosphorylation sites in the EMS1 inner juxtamembrane domain and six in vitro Ser and Thr phosphorylation sites in the EMS1 ATP-binding domain and activation loop.…”

Section: Discussionmentioning

confidence: 61%

“…In this study, we identified five in vitro Ser and Thr phosphorylation sites in the EMS1 inner juxtamembrane domain and six in vitro Ser and Thr phosphorylation sites in the EMS1 ATP-binding domain and activation loop. Phosphorylation occurs in both conserved and nonconserved residues in LRR-RLKs (Mitra et al, 2015). Similarly, alignment of the EMS1-CD with its most related LRR-RLKs (BRI1, BRL1, BRL2, and BRL3) shows that only the Ser-892, Thr-914, and Ser-1076 phosphorylation sites are conserved, but nine other phosphorylation sites are diverse (Supplemental Fig.…”

Section: Discussionmentioning

confidence: 87%

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Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination

Wang

Huang

et al. 2016

Plant Physiol.

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Cell signaling pathways mediated by leucine-rich repeat receptor-like kinases (LRR-RLKs) are essential for plant growth, development, and defense. The EMS1 (EXCESS MICROSPOROCYTES1) LRR-RLK and its small protein ligand TPD1 (TAPETUM DETERMINANT1) play a fundamental role in somatic and reproductive cell differentiation during early anther development in Arabidopsis (Arabidopsis thaliana). However, it is unclear whether other cell surface molecules serve as coregulators of EMS1. Here, we show that SERK1 (SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1) and SERK2 LRR-RLKs act redundantly as coregulatory and physical partners of EMS1. The SERK1/2 genes function in the same genetic pathway as EMS1 in anther development. Bimolecular fluorescence complementation, Förster resonance energy transfer, and coimmunoprecipitation approaches revealed that SERK1 interacted biochemically with EMS1. Transphosphorylation of EMS1 by SERK1 enhances EMS1 kinase activity. Among 12 in vitro autophosphorylation and transphosphorylation sites identified by tandem mass spectrometry, seven of them were found to be critical for EMS1 autophosphorylation activity. Furthermore, complementation test results suggest that phosphorylation of EMS1 is required for its function in anther development. Collectively, these data provide genetic and biochemical evidence of the interaction and phosphorylation between SERK1/2 and EMS1 in anther development.

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Section: Discussionsupporting

confidence: 51%

Section: Discussionmentioning

confidence: 61%

Section: Discussionmentioning

confidence: 87%

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Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination

Wang

Huang

et al. 2016

Plant Physiol.

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“…The fourth phosphosite of MtLYR3 (Ser399) is located just after the predicted aC-helix, which is a key structural element in the N-terminal lobe of protein kinases [42]. The fifth phosphosite (Thr628) is located in the C-terminal domain of the protein, a region commonly subjected to phosphorylation [43], including in vivo for MtLYR4 and the Arabidopsis LRR-RLK, AtBRI1 [35,44]. Taken together, the phosphorylation of MtLYR3 by MtLYK3 revealed the existence of phosphosites that could be of relevance in a biological context.…”

Section: Discussionmentioning

confidence: 99%

LYR3, a high‐affinity LCO‐binding protein of Medicago truncatula, interacts with LYK3, a key symbiotic receptor

et al. 2016

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Edited by Julian Schroeder LYR3, LYK3, and NFP are lysin motif-containing receptor-like kinases (LysM-RLKs) from Medicago truncatula, involved in perception of symbiotic lipo-chitooligosaccharide (LCO) signals. Here, we show that LYR3, a highaffinity LCO-binding protein, physically interacts with LYK3, a key player regulating symbiotic interactions. In vitro, LYR3 is phosphorylated by the active kinase domain of LYK3. Fluorescence lifetime imaging/F€ orster resonance energy transfer (FLIM/FRET) experiments in tobacco protoplasts show that the interaction between LYR3 and LYK3 at the plasma membrane is disrupted or inhibited by addition of LCOs. Moreover, LYR3 attenuates the cell death response, provoked by coexpression of NFP and LYK3 in tobacco leaves.Keywords: FLIM/FRET; lipo-chitooligosaccharides; LysM-RLK; Medicago truncatula; membrane receptor complex; phosphoproteomics The extracellular domains of plant RLKs are built up of different protein domains which serve as sensors for endogenous and outer stimuli, as diverse as peptides, hormones, (peptido-) glycans, and (lipo-) chitooligosaccharides. Two prevalent extracellular protein domains consist of either leucine-rich repeats (LRRs) or lysin motifs (LysMs), which might interact with peptides or with N-acetyl-D-glucosamine (GlcNAc)-containing compounds, respectively [1,2].Recent advances in functional and structural analyses of plant RLKs, particularly in Arabidopsis, suggest that plant RLKs act in multimeric complexes [3]. For example, the LysM-RLK chitin elicitor receptor kinase 1 of A. thaliana (AtCERK1) interacts with other receptor proteins to mediate responses to different signals. This protein can bind chitooligosaccharides (COs) [4], but it also interacts with two CO-binding LysM-RLKs with dead kinase domains (AtLYK5/ AtLYK4) [5] and with two peptidoglycan-binding LysM receptor-like proteins (AtLYM1/AtLYM3) [6] to mediate defense responses to these GlcNAc-containing signals. In contrast, OsCERK1 from rice

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“…To identify kinase(s) that phosphorylate a tyrosine residue on AtGPA1, we purified 70 recombinant LRR RLKs, containing the intracellular juxtamembrane, the catalytic kinase and the C-terminal domains (48). We biochemically screened these kinases for AtGPA1 substrate specificity ( Fig.…”

Section: Identification Of 18 Atgpa1 Kinases One Requires Y166 For Amentioning

confidence: 99%

Tyrosine phosphorylation switching of a G protein

Li¹,

Tunc‐Ozdemir²,

Urano

et al. 2018

Journal of Biological Chemistry

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Heterotrimeric G protein complexes are molecular switches relaying extracellular signals sensed by G protein-coupled receptors (GPCRs) to downstream targets in the cytoplasm, which effect cellular responses. In the plant heterotrimeric GTPase cycle, GTP hydrolysis, rather than nucleotide exchange, is the rate-limiting reaction and is accelerated by a receptor-like regulator of G signaling (RGS) protein. We hypothesized that posttranslational modification of the Gα subunit in the G-protein complex regulates the RGSdependent GTPase cycle. Our structural analyses identified an invariant phosphorylated tyrosine residue (Tyr-166 in the Arabidopsis Gα subunit AtGPA1) located in the intramolecular domain interface where nucleotide binding and hydrolysis occurs. We also identified a receptor-like kinase that phosphorylates AtGPA1 in a Tyr-166-dependent manner. Discrete molecular dynamics simulations predicted that phosphorylated Tyr-166 forms a salt bridge in this interface and potentially affects the RGS protein-accelerated GTPase cycle. Using a Tyr-166 phosphomimetic substitution, we found that the cognate RGS protein binds more tightly to the GDP-bound Gα substrate, consequently reducing its ability to accelerate GTPase activity. In conclusion, we propose that phosphorylation of Tyr-166 in AtGPA1 changes the binding pattern with AtRGS1 and thereby attenuates the steady-state rate of the GTPase cycle. We coin this newly identified mechanism "substrate phosphoswitching." __________________________________ http://www.jbc.org/cgi

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An autophosphorylation site database for leucine‐rich repeat receptor‐like kinases in Arabidopsis thaliana

Cited by 36 publications

References 62 publications

Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination

Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination

LYR3, a high‐affinity LCO‐binding protein of Medicago truncatula, interacts with LYK3, a key symbiotic receptor

Tyrosine phosphorylation switching of a G protein

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