A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity
By Dongping Lu, Shujing Wu, Xiquan Gao, Yulan Zhang, Libo Shan, Ping He. Proceedings of the National Academy of Sciences of the United States of America, 2009
804 citations recorded by the source corpus.
Subfields: Plant Science
View Paper: https://www.semanticscholar.org/paper/663a55911dc979c59ad6390aad62265fe518a271
How researchers see this paper
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In Plant Science
- Cyril Zipfel
- Heribert Hirt
- Alok Kumar Pandey
- Subhadeep Chatterjee
- J. Colcombet
- S. He
- Jonathan D. G. Jones
- Ping He
Citations in the corpus
- The FLS2-associated kinase BIK1 directly phosphorylates the NADPH oxidase RbohD to control plant immunity. (2014, background): “BIK1 and PBL1 are two highly homologous receptor-like cytoplasmic kinases that play an additive role in defenses by associating with the unstimulated FLS2 and other PRRs (Lu et al., 2010; Zhang et al., 2010).”
- Direct ubiquitination of pattern recognition receptor FLS2 attenuates plant innate immunity (2011, methodology): “Expression of the GST and MBP fusion proteins and affinity purification were performed as standard protocol, and in vitro phosphorylation and immunocomplex kinase assays were carried out as described (11).”
- Plant pattern recognition receptor complexes at the plasma membrane. (2012, background): “BIK1 and the paralogous proteins PBS1, PBL1, and PBL2 associate constitutively with FLS2 and potentially with BAK1 [59 ,60 ].”
- Plant immunity: towards an integrated view of plant–pathogen interactions (2010, neutral): “In vivo , BIK1 becomes phosphorylated 5–10 min after treatment with flagelli”
- Signaling mechanisms in pattern-triggered immunity (PTI). (2015, background): “In addition to BAK1, the receptor-like cytoplasmic kinase Botrytis-induced kinase 1 (BIK1) and related PBL (PBS1like) kinases constitutively associate with FLS2 and EFR and become quickly phosphorylated and released from the PRR complexes upon MAMP binding (Lu et al., 2010; Zhang et al., 2010).”
- Direct regulation of the NADPH oxidase RBOHD by the PRR-associated kinase BIK1 during plant immunity. (2014, methodology): “In addition to BAK1, FLS2 and EFR constitutively associate with the receptor-like cytoplasmic kinases (RLCKs) BIK1 and related PBL proteins, which become rapidly phosphorylated and released from the FLS2 and EFR complexes upon PAMP perception (Lu et al., 2010; Zhang et al., 2010; Liu et al., 2013).”
- Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a Pseudomonas syringae effector. (2010, result): “Following the submission of this work, Lu et al. (2010) reported a flg22-induced phosphorylation of BIK1 which is largely consistent with our findings.”
- Signaling in Plant-Microbe Interactions (2013, background): “This indicates that BIK1 is an important component in PTI signaling (Lu et al. 2010).”
- Growth-defense tradeoffs in plants: a balancing act to optimize fitness. (2014, positive): “Treatment with flg22, a bioactive 22-amino acid peptide derived from bacterial flagellin, activates the FLS2/BAK1 co-receptor complex and triggers a phosphorylation cascade, including the phosphorylation and displacement of BOTRYTIS-INDUCED KINASE 1 (BIK1) from the FLS2 complex to promote the immune”