<i>Arabidopsis</i> RTNLB1 and RTNLB2 Reticulon-Like Proteins Regulate Intracellular Trafficking and Activity of the FLS2 Immune Receptor

Lee, Hyoung Yool; Bowen, C. Vaughan A.; Popescu, George V.; Kang, Hong-Gu; Kato, Naohiro; Ma, Shisong; Dinesh‐Kumar, Savithramma P.; Snyder, M; Popescu, S.

doi:10.1105/tpc.111.089656

Cited by 69 publications

(66 citation statements)

References 105 publications

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“…As FLS2 is predominantly localized in the PM before activation 34 , while the majority of CRT1 is in endomembranes 13 , an interesting question is where these immune proteins interact. Analyses of endoglycosidase H sensitivity 35 have suggested that FLS2, whether expressed in N. benthamiana or Arabidopsis, is present in both the endoplasmic reticulum and PM 36,37 . Moreover, a portion of FLS2 was found in endomembranes 36 , suggesting the CRT1-FLS2 interaction may occur in this compartment.…”

Section: Discussionmentioning

confidence: 99%

“…Analyses of endoglycosidase H sensitivity 35 have suggested that FLS2, whether expressed in N. benthamiana or Arabidopsis, is present in both the endoplasmic reticulum and PM 36,37 . Moreover, a portion of FLS2 was found in endomembranes 36 , suggesting the CRT1-FLS2 interaction may occur in this compartment. Supporting this possibility, the animal PRRs TLR9 and TLR4, key factors in modulating innate and adaptive immunity, require localization to endosomes for their functions 38,39 .…”

Section: Discussionmentioning

confidence: 99%

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CRT1 is a nuclear-translocated MORC endonuclease that participates in multiple levels of plant immunity

et al. 2012

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Arabidopsis thaliana CRT1 (compromised for recognition of Turnip Crinkle Virus) was previously shown to be required for effector-triggered immunity. Sequence analyses previously revealed that CRT1 contains the ATPase and S5 domains characteristic of Microchidia (MORC) proteins; these proteins are associated with DNA modification and repair. Here we show that CRT1 and its closest homologue, CRH1, are also required for pathogen-associated molecular pattern (PAMP)-triggered immunity, basal resistance, nonhost resistance and systemic acquired resistance. Consistent with its role in PAMP-triggered immunity, CRT1 interacted with the PAMP recognition receptor FLS2. Subcellular fractionation and transmission electron microscopy detected a subpopulation of CRT1 in the nucleus, whose levels increased following PAMP treatment or infection with an avirulent pathogen. These results, combined with the demonstration that CRT1 binds DNA, exhibits endonuclease activity, and affects tolerance to the DNA-damaging agent mitomycin C, argue that this prototypic eukaryotic member of the MORC superfamily has important nuclear functions during immune response activation.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

CRT1 is a nuclear-translocated MORC endonuclease that participates in multiple levels of plant immunity

et al. 2012

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“…Studies have shown that RTN family molecules could function in protein transport from the ER to other membrane compartments, including the plasma membrane, Golgi, and endosomes (40)(41)(42). For example, RTN2B enhances trafficking of glutamate transporter EAAC1 from the ER to the cell surface.…”

Section: Discussionmentioning

confidence: 99%

“…Nogo-A regulates redistribution of the ER-resident chaperone protein disulfide isomerase and contributes the proper function of protein disulfide isomerase (39). Studies have shown that some RTN family molecules could also function in protein transport from ER to other membrane compartments, including the plasma membrane, Golgi, and endosomes (40)(41)(42). For example, RTN2B enhances trafficking of glutamate transporter EAAC1 from the ER to the cell surface.…”

Section: Gramd4 Binds To Nogo-b and Inhibits Nucleic Acid-induced Tlrmentioning

confidence: 99%

Endoplasmic Protein Nogo-B (RTN4-B) Interacts with GRAMD4 and Regulates TLR9-Mediated Innate Immune Responses

Kimura

Endo

Inui

et al. 2015

The Journal of Immunology

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TLRs are distributed in their characteristic cellular or subcellular compartments to efficiently recognize specific ligands and to initiate intracellular signaling. Whereas TLRs recognizing pathogen-associated lipids or proteins are localized to the cell surface, nucleic acid–sensing TLRs are expressed in endosomes and lysosomes. Several endoplasmic reticulum (ER)–resident proteins are known to regulate the trafficking of TLRs to the specific cellular compartments, thus playing important roles in the initiation of innate immune responses. In this study, we show that an ER-resident protein, Nogo-B (or RTN4-B), is necessary for immune responses triggered by nucleic acid–sensing TLRs, and that a newly identified Nogo-B–binding protein (glucosyltransferases, Rab-like GTPase activators and myotubularins [GRAM] domain containing 4 [GRAMD4]) negatively regulates the responses. Production of inflammatory cytokines in vitro by macrophages stimulated with CpG-B oligonucleotides or polyinosinic:polycytidylic acid was attenuated in the absence of Nogo-B, which was also confirmed in serum samples from Nogo-deficient mice injected with polyinosinic:polycytidylic acid. Although a deficiency of Nogo-B did not change the incorporation or delivery of CpG to endosomes, the localization of TLR9 to endolysosomes was found to be impaired. We identified GRAMD4 as a downmodulator for TLR9 response with a Nogo-B binding ability in ER, because our knockdown and overexpression experiments indicated that GRAMD4 suppresses the TLR9 response and knockdown of Gramd4 strongly enhanced the response in the absence of Nogo-B. Our findings indicate a critical role of Nogo-B and GRAMD4 in trafficking of TLR9.

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“…Consequently, the sensitivity or resistance of N-glycans to Endo H digestion is commonly used as a convenient assay for determining if secreted glycoproteins contain complex N-glycans (i.e., show resistance to Endo H digestion), an indication that they have exited the ER and entered the Golgi apparatus on their way to the cell surface. In plants, sensitivity to Endo H digestion has been used to assess the subcellular localization of the BRASSINOSTEROID INSENSITIVE1 (Jin et al, 2007(Jin et al, , 2009Hong et al, 2008), FLAGELLIN SENSITIVE2 (FLS2) (Lee et al, 2011), and EFR (Nekrasov et al, 2009) receptors and specifically to assay for receptor exit from the ER.…”

Section: N-glycosylation Of Srkb Is Required For the Ability Of The Smentioning

confidence: 99%

Site-SpecificN-Glycosylation of the S-Locus Receptor Kinase and Its Role in the Self-Incompatibility Response of the Brassicaceae

et al. 2014

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The S-locus receptor kinase SRK is a highly polymorphic transmembrane kinase of the stigma epidermis. Through allelespecific interaction with its pollen coat-localized ligand, the S-locus cysteine-rich protein SCR, SRK is responsible for recognition and inhibition of self pollen in the self-incompatibility response of the Brassicaceae. The SRK extracellular ligand binding domain contains several potential N-glycosylation sites that exhibit varying degrees of conservation among SRK variants. However, the glycosylation status and functional importance of these sites are currently unclear. We investigated this issue in transgenic Arabidopsis thaliana stigmas that express the Arabidopsis lyrata SRKb variant and exhibit an incompatible response toward SCRb-expressing pollen. Analysis of single-and multiple-glycosylation site mutations of SRKb demonstrated that, although five of six potential N-glycosylation sites in SRKb are glycosylated in stigmas, N-glycosylation is not important for SCRb-dependent activation of SRKb. Rather, N-glycosylation functions primarily to ensure the proper and efficient subcellular trafficking of SRK to the plasma membrane. The study provides insight into the function of a receptor that regulates a critical phase of the plant life cycle and represents a valuable addition to the limited information available on the contribution of N-glycosylation to the subcellular trafficking and function of plant receptor kinases.

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Arabidopsis RTNLB1 and RTNLB2 Reticulon-Like Proteins Regulate Intracellular Trafficking and Activity of the FLS2 Immune Receptor

Cited by 69 publications

References 105 publications

CRT1 is a nuclear-translocated MORC endonuclease that participates in multiple levels of plant immunity

CRT1 is a nuclear-translocated MORC endonuclease that participates in multiple levels of plant immunity

Endoplasmic Protein Nogo-B (RTN4-B) Interacts with GRAMD4 and Regulates TLR9-Mediated Innate Immune Responses

Site-SpecificN-Glycosylation of the S-Locus Receptor Kinase and Its Role in the Self-Incompatibility Response of the Brassicaceae

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