Functional importance of BAK1 tyrosine phosphorylation in vivo

Oh, Man‐Ho; Wu, Xia; Clouse, Steven D.

doi:10.4161/psb.6.3.14337

Cited by 21 publications

(21 citation statements)

References 42 publications

(50 reference statements)

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“…Such YXXɸ internalization motif is present in BAK1 but absent from FLS2. Despite the fact that BAK1 contains a YXXɸ motif (Geldner et al, 2007) and shows Tyr phosphorylation required for some flg22-signaling responses (Oh et al, 2010(Oh et al, , 2011, our chemical interference results in Col-0 and bak1-4 plants indicated that BAK1 was unlikely the only target of TyrA23-dependent inhibition of flg22-induced ROS production. Thus, we propose that other, yet unknown YXXɸ-containing protein(s) or component(s) targeted by TyrA23 or Wm appear to participate in flg22-induced ROS production that function either downstream of or in a parallel pathway to BAK1.…”

Section: Discussionmentioning

confidence: 91%

“…0.15). Notably, BAK1 undergoes Tyr phosphorylation required for flg22 signaling (Oh et al, 2010(Oh et al, , 2011, and BAK1, but not FLS2, contains a YXXɸ motif in its cytoplasmic tail (Geldner and Robatzek, 2008;Robatzek and Wirthmueller, 2013), thus raising the possibility that BAK1 may be the target of the observed TyrA23-dependent inhibitory effects on flg22-ROS production in Col-0. To this end, we directly compared ROS production in Col-0 and bak1-4 leaf strips that were either pretreated with TyrA23 (+TyrA23) or mock pretreated (-TyrA23) prior to their elicitation with 1 mM flg22.…”

Section: Vesicular Trafficking Inhibitors Impede Ligand-induced Degramentioning

confidence: 99%

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Sensitivity to Flg22 Is Modulated by Ligand-Induced Degradation and de Novo Synthesis of the Endogenous Flagellin-Receptor FLAGELLIN-SENSING2

et al. 2013

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FLAGELLIN-SENSING2 (FLS2) is the plant cell surface receptor that perceives bacterial flagellin or flg22 peptide, initiates flg22-signaling responses, and contributes to bacterial growth restriction. Flg22 elicitation also leads to ligand-induced endocytosis and degradation of FLS2 within 1 h. Why plant cells remove this receptor precisely at the time during which its function is required remains mainly unknown. Here, we assessed in planta flg22-signaling competency in the context of ligand-induced degradation of endogenous FLS2 and chemical interference known to impede flg22-dependent internalization of FLS2 into endocytic vesicles. Within 1 h after an initial flg22 treatment, Arabidopsis (Arabidopsis thaliana) leaf tissue was unable to reelicit flg22 signaling in a ligand-, time-, and dose-dependent manner. These results indicate that flg22-induced degradation of endogenous FLS2 may serve to desensitize cells to the same stimulus (homologous desensitization), likely to prevent continuous signal output upon repetitive flg22 stimulation. In addition to impeding ligand-induced FLS2 degradation, pretreatment with the vesicular trafficking inhibitors Wortmannin or Tyrphostin A23 impaired flg22-elicited reactive oxygen species production that was partially independent of BRASSINOSTEROID INSENSITIVE1-ASSOCIATED KINASE1. Interestingly, these inhibitors did not affect flg22-induced mitogenactivated protein kinase phosphorylation, indicating the ability to utilize vesicular trafficking inhibitors to target different flg22-signaling responses. For Tyrphostin A23, reduced flg22-induced reactive oxygen species could be separated from the defect in FLS2 degradation. At later times (.2 h) after the initial flg22 elicitation, recovery of FLS2 protein levels positively correlated with resensitization to flg22, indicating that flg22-induced new synthesis of FLS2 may prepare cells for a new round of monitoring the environment for flg22.

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Section: Discussionmentioning

confidence: 91%

Section: Vesicular Trafficking Inhibitors Impede Ligand-induced Degramentioning

confidence: 99%

Sensitivity to Flg22 Is Modulated by Ligand-Induced Degradation and de Novo Synthesis of the Endogenous Flagellin-Receptor FLAGELLIN-SENSING2

et al. 2013

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“…Animal receptor kinases are predominantly tyrosine kinases, whereas plant receptor kinases are generally classified as Ser/Thr kinases, although recent work suggests that some plant receptor kinases are dual-specificity kinases that can also autophosphorylate on tyrosine residues (2)(3)(4)(5). One of the best-studied plant receptor kinases is BRASSINOSTEROID INSENSITIVE 1 (BRI1), which functions with its coreceptor, BRI1-ASSOCIATED RECEPTOR KINASE 1 (BAK1), in brassinosteroid (BR) signaling (6)(7)(8)(9)(10)(11).…”

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confidence: 99%

Deactivation of the Arabidopsis BRASSINOSTEROID INSENSITIVE 1 (BRI1) receptor kinase by autophosphorylation within the glycine-rich loop

Wang

Clouse

2011

Proc. Natl. Acad. Sci. U.S.A.

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The activity of the dual-specificity receptor kinase, brassinosteroid insensitive 1 (BRI1), reflects the balance between phosphorylationdependent activation and several potential mechanisms for deactivation of the receptor. In the present report, we elucidate a unique mechanism for deactivation that involves autophosphorylation of serine-891 in the ATP-binding domain. Serine-891 was identified previously as a potential site of autophosphorylation by mass spectrometry, and sequence-specific antibodies and mutagenesis studies now unambiguously establish phosphorylation of this residue. In vivo, phosphorylation of serine-891 increased slowly with time following application of brassinolide (BL) to Arabidopsis seedlings, whereas phosphorylation of threonine residues increased rapidly and then remained constant. Transgenic plants expressing the BRI1(S891A)-Flag-directed mutant have increased hypocotyl and petiole lengths, relative to wild-type BRI1-Flag (both in the bri1-5 background), and accumulate higher levels of the unphosphorylated form of the BES1 transcription factor in response to exogenous BL. In contrast, plants expressing the phosphomimetic S891D-directed mutant are severely dwarfed and do not accumulate unphosphorylated BES1 in response to BL. Collectively, these results suggest that autophosphorylation of serine-891 is one of the deactivation mechanisms that inhibit BRI1 activity and BR signaling in vivo. Many arginine-aspartate (RD)-type leucine-rich repeat receptor-like kinases have a phosphorylatable residue within the ATP-binding domain, suggesting that this mechanism may play a broad role in receptor kinase deactivation.T he receptor-like kinase (RLK) family in Arabidopsis contains more than 600 members, of which more than 400 are structurally and functionally similar to animal receptor kinases but are evolutionarily distinct (1). Animal receptor kinases are predominantly tyrosine kinases, whereas plant receptor kinases are generally classified as Ser/Thr kinases, although recent work suggests that some plant receptor kinases are dual-specificity kinases that can also autophosphorylate on tyrosine residues (2-5). One of the best-studied plant receptor kinases is BRASSINOSTEROID INSENSITIVE 1 (BRI1), which functions with its coreceptor, BRI1-ASSOCIATED RECEPTOR KINASE 1 (BAK1), in brassinosteroid (BR) signaling (6-11). Current thinking is that BRI1 and BAK1 are in their unphosphorylated forms and inactive in the absence of BR, whereas in the presence of the BR ligand, BRI1 and BAK1 heterodimerize and become activated via auto-and transphosphorylation (12). The BRI1 KINASE INHIBITOR 1 (BKI1) and the BR-signaling kinase 1 (BSK1) may be two of the immediate downstream components that are first phosphorylated by BRI1 (13,14). BSK then activates the BRI1 SUPPRESSOR 1 (BSU1) phosphatase (15), which in turn inhibits the glycogen synthase 3-like protein kinase, BRASSINOSTEROID INSENSITIVE 2 (BIN2), by dephosphorylation of an essential phosphotyrosine residue (16). The net result is that the transcription fac...

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“…This was initially demonstrated for several members of the large receptor-like kinase family in Arabidopsis 21 - 26 and a similar situation appears to be emerging with the CDPK family. One clear conclusion is that we do not have an adequate understanding of the kinase domain motifs that confer (or predict) dual specificity.…”

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confidence: 60%

Impact of Ca²⁺on structure of soybean CDPKβ and accessibility of the Tyr-24 autophosphorylation site

2013

Plant Signaling & Behavior

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Several plant CDPKs were recently shown to be dual specificity kinases rather than Ser/Thr kinases as traditionally classified by sequence analysis. In the present study we confirm the autophosphorylation of recombinant soybean His6-GmCDPKβ at the Tyr-24 site using sequence- and modification- specific antibodies. Homology modeling of soybean CDPKβ based on recent structures determined for several apicomplexan CDPKs suggested that phosphotyrosine-24 may be inaccessible to phosphatases. However, we report that dephosphorylation of CDPKβ by the protein tyrosine phosphatase 1B, PTP1B, was not restricted in the presence of calcium. Thus, despite conformational changes likely associated with calcium binding to the CDPKs, phosphotyrosine sites remain fully accessible to dephosphorylation suggesting the possibility of conformational breathing and flexing.

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Functional importance of BAK1 tyrosine phosphorylation in vivo

Cited by 21 publications

References 42 publications

Sensitivity to Flg22 Is Modulated by Ligand-Induced Degradation and de Novo Synthesis of the Endogenous Flagellin-Receptor FLAGELLIN-SENSING2

Sensitivity to Flg22 Is Modulated by Ligand-Induced Degradation and de Novo Synthesis of the Endogenous Flagellin-Receptor FLAGELLIN-SENSING2

Deactivation of the Arabidopsis BRASSINOSTEROID INSENSITIVE 1 (BRI1) receptor kinase by autophosphorylation within the glycine-rich loop

Impact of Ca²⁺on structure of soybean CDPKβ and accessibility of the Tyr-24 autophosphorylation site

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Functional importance of BAK1 tyrosine phosphorylation in vivo

Cited by 21 publications

References 42 publications

Sensitivity to Flg22 Is Modulated by Ligand-Induced Degradation and de Novo Synthesis of the Endogenous Flagellin-Receptor FLAGELLIN-SENSING2

Sensitivity to Flg22 Is Modulated by Ligand-Induced Degradation and de Novo Synthesis of the Endogenous Flagellin-Receptor FLAGELLIN-SENSING2

Deactivation of the Arabidopsis BRASSINOSTEROID INSENSITIVE 1 (BRI1) receptor kinase by autophosphorylation within the glycine-rich loop

Impact of Ca2+on structure of soybean CDPKβ and accessibility of the Tyr-24 autophosphorylation site

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Impact of Ca²⁺on structure of soybean CDPKβ and accessibility of the Tyr-24 autophosphorylation site