Recruitment of PLANT U-BOX13 and the PI4Kβ1/β2 Phosphatidylinositol-4 Kinases by the Small GTPase RabA4B Plays Important Roles during Salicylic Acid-Mediated Plant Defense Signaling in Arabidopsis

Antignani, Vincenzo; Klocko, Amy L.; Bak, Gwangbae; Chandrasekaran, Suma D.; Dunivin, Taylor K; Nielsen, Erik

doi:10.1105/tpc.114.134262

Cited by 87 publications

(81 citation statements)

References 84 publications

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“…Multiple lines of evidence suggest that it does: i) PI4Kβs localize in endosomes 45,46 and ii) several Arabidopsis proteins that bind PI4P also localize in endomembranes 47,48 . However, similar to PH FAPP1 , these proteins also bind both PI4P and endosomal small GTPases 47,48 . In addition, we show that PI4P-binding domains that localizes specifically to the PM, also localizes to endomembranes upon depletion of the PI4P PM pool.…”

Section: Discussionmentioning

confidence: 99%

A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants

Simon¹,

Platre²,

et al. 2016

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Many signaling proteins permanently or transiently localize to specific organelles for function. It is well established that certain lipids act as biochemical landmarks to specify compartment identity. However, they also influence membrane biophysical properties, which emerge as important features in specifying cellular territories. Such parameters include the membrane inner surface potential, which varies according to the lipid composition of each organelle. Here, we found that the plant plasma membrane (PM) and the cell plate of dividing cells have a unique electrostatic signature controlled by phosphatidylinositol-4-phosphate (PI4P). Our results further reveal that, contrarily to other eukaryotes, PI4P massively accumulates at the PM, establishing it as a critical hallmark of this membrane in plants. Membrane surface charges control the PM localization and function of the polar auxin transport regulator PINOID, as well as proteins from the BRI1 KINASE INHIBITOR1 (BKI1)/MEMBRANE ASSOCIATED KINASE REGULATORs (MAKRs) family, which are involved in brassinosteroid and receptor-like kinase signaling. We anticipate that this PI4P-driven physical membrane property will control the localization and function of many proteins involved in development, reproduction, immunity and nutrition.

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Section: Discussionmentioning

confidence: 99%

A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants

Simon¹,

Platre²,

et al. 2016

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“…These results indicate that EREX must interact with both canonical RAB5 and the phosphoinositide to be efficiently recruited to the endosomal membrane. Although phosphoinositide metabolism on the endosomes has not been directly linked to RAB5 in plants, our results suggest that canonical RAB5 functions in close association with phosphoinositides, as is the case for other plant RAB GTPases and animal RAB5 (Grosshans et al, 2006;Preuss et al, 2006;Camacho et al, 2009;Antignani et al, 2015). (A) Four-day-old erex erel1 and EREX EREL1 plants were treated with DMSO or 33 mM wortmannin for 100 min.…”

Section: Structural Features Of Erex/erel Membersmentioning

confidence: 99%

ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an Interacting Partner of RAB5 GTPases, Regulates Membrane Trafficking to Protein Storage Vacuoles in Arabidopsis

et al. 2016

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ORCID ID: 0000-0001-7441-0203 (H.T.S.)RAB5 GTPases act as molecular switches that regulate various endosomal functions in animal cells, including homotypic fusion of early endosomes, endosomal motility, endosomal signaling, and subcompartmentalization of the endosomal membrane. RAB5 proteins fulfill these diverse functions through interactions with downstream effector molecules. Two canonical RAB5 members, ARA7 and RAB HOMOLOG1 (RHA1), are encoded in the Arabidopsis thaliana genome. ARA7 and RHA1 play crucial roles in endocytic and vacuolar trafficking pathways. Plant RAB5 GTPases function via interactions with effector molecules, whose identities and functions are currently unclear. In this study, we searched for canonical RAB5 effector molecules of Arabidopsis and identified a candidate, which we called ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN (EREX). The intimate genetic interaction between EREX and RAB5 members, the results from subcellular colocalization experiments, and the direct interaction observed in an in vitro pull-down assay strongly suggest that EREX is a genuine effector of canonical RAB5s in Arabidopsis. We further found that close homologs of EREX play partially redundant functions with EREX in the transport of seed storage proteins. Our results indicate that canonical plant RAB5s acquired distinct effector molecules from those of non-plant systems to fulfill their functions.

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“…The E3 ligases PUB12 and PUB13 both work to attenuate PTI by ubiquitinating the flg22 receptor FLS2, facilitating its degradation (Lu et al, 2011). Recent Y2H screens have revealed potential coregulatory partners and substrates for ubiquitination by PUB13, including phosphatidylinositol-4 kinase and RABA4B, with which it complexes to negatively regulate salicylic acid-mediated defenses (Antignani et al, 2015), and the abscisic acid regulator ABI1, a PP2C family member, which is a PUB13 substrate for ubiquitination and degradation (Kong et al, 2015). In addition, PUB22, PUB23, and PUB24 also suppress immunity.…”

Section: Stnrl1 Overexpression Suppresses Inf1-mediated Cell Death Anmentioning

confidence: 99%

Potato NPH3/RPT2-Like Protein StNRL1, Targeted by a Phytophthora infestans RXLR Effector, Is a Susceptibility Factor

et al. 2016

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Plant pathogens deliver effectors to manipulate host processes. We know little about how fungal and oomycete effectors target host proteins to promote susceptibility, yet such knowledge is vital to understand crop disease. We show that either transient expression in Nicotiana benthamiana, or stable transgenic expression in potato (Solanum tuberosum), of the Phytophthora infestans RXLR effector Pi02860 enhances leaf colonization by the pathogen. Expression of Pi02860 also attenuates cell death triggered by the P. infestans microbeassociated molecular pattern INF1, indicating that the effector suppresses pattern-triggered immunity. However, the effector does not attenuate cell death triggered by Cf4/Avr4 coexpression, showing that it does not suppress all cell death activated by cell surface receptors. Pi02860 interacts in yeast two-hybrid assays with potato NPH3/RPT2-LIKE1 (NRL1), a predicted CULLIN3-associated ubiquitin E3 ligase. Interaction of Pi02860 in planta was confirmed by coimmunoprecipitation and bimolecular fluorescence complementation assays. Virus-induced gene silencing of NRL1 in N. benthamiana resulted in reduced P. infestans colonization and accelerated INF1-mediated cell death, indicating that this host protein acts as a negative regulator of immunity. Moreover, whereas NRL1 virus-induced gene silencing had no effect on the ability of the P. infestans effector Avr3a to suppress INF1-mediated cell death, such suppression by Pi02860 was significantly attenuated, indicating that this activity of Pi02860 is mediated by NRL1. Transient overexpression of NRL1 resulted in the suppression of INF1-mediated cell death and enhanced P. infestans leaf colonization, demonstrating that NRL1 acts as a susceptibility factor to promote late blight disease.

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Recruitment of PLANT U-BOX13 and the PI4Kβ1/β2 Phosphatidylinositol-4 Kinases by the Small GTPase RabA4B Plays Important Roles during Salicylic Acid-Mediated Plant Defense Signaling in Arabidopsis

Cited by 87 publications

References 84 publications

A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants

A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants

ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an Interacting Partner of RAB5 GTPases, Regulates Membrane Trafficking to Protein Storage Vacuoles in Arabidopsis

Potato NPH3/RPT2-Like Protein StNRL1, Targeted by a Phytophthora infestans RXLR Effector, Is a Susceptibility Factor

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