2014
DOI: 10.1093/mp/ssu003
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An XA21-Associated Kinase (OsSERK2) Regulates Immunity Mediated by the XA21 and XA3 Immune Receptors

Abstract: SUMMARYWe show that OsSERK2 is a regulator of innate immune signaling mediated by multiple non-RD receptor kinases (RKs) including XA21, XA3, and OsFLS2. OsSerk2-silenced rice lines are impaired in XA21-mediated immunity to Xoo PXO99, XA3-mediated immunity to Xoo PXO86, and OsFLS2-mediated defense responses. Thus, OsSERK2 is broadly involved in PRR-mediated immunity in rice.

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Cited by 140 publications
(221 citation statements)
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References 84 publications
(198 reference statements)
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“…The SERK proteins have also been shown to serve various other BR-independent functions by forming heterocomplexes with SG_XIIa receptors (FLS2 and EFR, structure O in Figure 5 ) and the PEP1 RECEPTOR proteins (PEPR1, SG_XI N4 in Figure 5 ) (Chinchilla et al, 2007; Heese et al, 2007; Albrecht et al, 2008; Schulze et al, 2010; Roux et al, 2011; Koller and Bent, 2014). In rice, OsSERK2 (SG_II B.3 in Figure 5 ) forms a constitutive complex with the LRR-RLK Xa21 (SG_XIIa O in Figure 5 ) (Chen et al, 2014). Thus, these SERK co-receptors (4-5 LRRs) seem to play a central role in the regulation of multiple LRR-RLKs (>20 LRRs) by interacting directly with them (Aker and de Vries, 2008; Chinchilla et al, 2009; Kim et al, 2013; Santiago et al, 2013; Sun et al, 2013).…”
Section: Resultsmentioning
confidence: 99%
“…The SERK proteins have also been shown to serve various other BR-independent functions by forming heterocomplexes with SG_XIIa receptors (FLS2 and EFR, structure O in Figure 5 ) and the PEP1 RECEPTOR proteins (PEPR1, SG_XI N4 in Figure 5 ) (Chinchilla et al, 2007; Heese et al, 2007; Albrecht et al, 2008; Schulze et al, 2010; Roux et al, 2011; Koller and Bent, 2014). In rice, OsSERK2 (SG_II B.3 in Figure 5 ) forms a constitutive complex with the LRR-RLK Xa21 (SG_XIIa O in Figure 5 ) (Chen et al, 2014). Thus, these SERK co-receptors (4-5 LRRs) seem to play a central role in the regulation of multiple LRR-RLKs (>20 LRRs) by interacting directly with them (Aker and de Vries, 2008; Chinchilla et al, 2009; Kim et al, 2013; Santiago et al, 2013; Sun et al, 2013).…”
Section: Resultsmentioning
confidence: 99%
“…Thus, the binding of FLS2 to flg22 recruits BAK1 to form a heterodimer, resulting in rapid phosphorylation of both FLS2 and BAK1 (Chinchilla et al, 2007;Heese et al, 2007;Schulze et al, 2010;Roux et al, 2011). Molecular and genetic studies showed that SERKs are also recruited to EFR, PEPRs, and Xa21 upon ligand binding and required for signaling (Roux et al, 2011;Chen et al, 2014;Yamada et al, 2016a). In addition, LRR-RKs for peptide hormones, including tracheary element differentiation inhibitory factor (TDIF), INFLORESCENCE DEFIECIENT IN ABSCISSION (IDA), PHYTOSULFOKINE (PSK), and ROOT GROWTH FACTORS (RGFs), also require SERKs for function Tang et al, 2015;Song et al, 2016;Santiago et al, 2016;Zhang et al, 2016).…”
Section: Ligand Binding and Oligomerization Of Prr Receptor Complexesmentioning
confidence: 99%
“…Similarly, reduced expression was not observed in the XA21 signaling components OsSERK2, XB3, XB15, XB21, or XB24, indicating that LRR1Ri specifically reduced Xa21 transcript levels. To determine if silencing of OsSERK2 also reduces Xa21 transcript levels, we compared Xa21 expression between XA21 rice and a homozygous line expressing an OsSERK2 silencing construct (XA21-OsSERKRi) (Chen et al 2014). No statistical difference in Xa21 expression was detected, indicating that silencing of OsSERK2 does not significantly reduce Xa21 transcript levels (Additional file 8: Figure S8).
Fig.
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Section: Resultsmentioning
confidence: 99%