StRemorin1.3 hampers <i>Potato virus X</i> TGBp1 ability to increase plasmodesmata permeability, but does not interfere with its silencing suppressor activity

Perraki, Artemis; Binaghi, María Julieta; Mecchia, Martín A.; Gronnier, Julien; German-Retana, Sylvie; Mongrand, Sébastien; Bayer, Emmanuelle; Zelada, Alicia M.; Germain, V.

doi:10.1016/j.febslet.2014.03.014

Cited by 56 publications

(70 citation statements)

References 37 publications

(60 reference statements)

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“…REMs form a large plant-specific protein family with characteristic PM nanodomain localisation patterns (Jarsch et al, 2014). Moreover, different members of this family have previously been associated with plant-microbe interactions (Raffaele et al, 2009; Lefebvre et al, 2010; Tóth et al, 2012; Perraki et al, 2012, 2014; Bozkurt et al, 2014) and with SERK-dependent processes (Gui et al, 2016). …”

Section: Resultsmentioning

confidence: 99%

Plant immune and growth receptors share common signalling components but localise to distinct plasma membrane nanodomains

Bücherl

Jarsch

Schudoma

et al. 2017

eLife

206

198

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Cell surface receptors govern a multitude of signalling pathways in multicellular organisms. In plants, prominent examples are the receptor kinases FLS2 and BRI1, which activate immunity and steroid-mediated growth, respectively. Intriguingly, despite inducing distinct signalling outputs, both receptors employ common downstream signalling components, which exist in plasma membrane (PM)-localised protein complexes. An important question is thus how these receptor complexes maintain signalling specificity. Live-cell imaging revealed that FLS2 and BRI1 form PM nanoclusters. Using single-particle tracking we could discriminate both cluster populations and we observed spatiotemporal separation between immune and growth signalling platforms. This finding was confirmed by visualising FLS2 and BRI1 within distinct PM nanodomains marked by specific remorin proteins and differential co-localisation with the cytoskeleton. Our results thus suggest that signalling specificity between these pathways may be explained by the spatial separation of FLS2 and BRI1 with their associated signalling components within dedicated PM nanodomains.DOI: http://dx.doi.org/10.7554/eLife.25114.001

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Section: Resultsmentioning

confidence: 99%

Plant immune and growth receptors share common signalling components but localise to distinct plasma membrane nanodomains

Bücherl

Jarsch

Schudoma

et al. 2017

eLife

206

198

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“…The mislocalization of these two GPI-anchored PD proteins results in an excessive amount of PDC deposition. Additionally, disruption in lipid rafts can affect the targeting of other lipid raft–enriched proteins such as Grain setting defect1 (GSD1), Remorins (REMs) and StRemorin1.3 which modulates PDC levels [82,83,84]. It was shown that GSD1 regulates PD conductance by interacting with ACTIN in association with the PDCB [84].…”

Section: Discussionmentioning

confidence: 99%

Lipid Raft, Regulator of Plasmodesmal Callose Homeostasis

Iswanto

Kim

2017

Plants

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The specialized plasma membrane microdomains known as lipid rafts are enriched by sterols and sphingolipids. Lipid rafts facilitate cellular signal transduction by controlling the assembly of signaling molecules and membrane protein trafficking. Another specialized compartment of plant cells, the plasmodesmata (PD), which regulates the symplasmic intercellular movement of certain molecules between adjacent cells, also contains a phospholipid bilayer membrane. The dynamic permeability of plasmodesmata (PDs) is highly controlled by plasmodesmata callose (PDC), which is synthesized by CALLOSE SYNTHASES (CalS) and degraded by β-1,3-GLUCANASES (BGs). In recent studies, remarkable observations regarding the correlation between lipid raft formation and symplasmic intracellular trafficking have been reported, and the PDC has been suggested to be the regulator of the size exclusion limit of PDs. It has been suggested that the alteration of lipid raft substances impairs PDC homeostasis, subsequently affecting PD functions. In this review, we discuss the substantial role of membrane lipid rafts in PDC homeostasis and provide avenues for understanding the fundamental behavior of the lipid raft–processed PDC.

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“…The atsrp1_1 (SALK_148081) and atsrp1_2 (GK-309G05) T-DNA mutants were obtained from the ABRC seed stock center, and homozygous lines were selected by PCR genotyping (primer sequences are provided in Table S1). For transient transformation, Nicotiana benthamiana leaves or 4-day-old A. thaliana seedlings were infiltrated with Agrobacterium tumefaciens cell cultures as described in Perraki et al (2014) or Marais et al (2015) respectively.…”

Section: Methodsmentioning

confidence: 99%

Proteomic Analysis of Lipid Droplets from Arabidopsis Aging Leaves Brings New Insight into Their Biogenesis and Functions

et al. 2017

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Lipid droplets (LDs) are cell compartments specialized for oil storage. Although their role and biogenesis are relatively well documented in seeds, little is known about their composition, structure and function in senescing leaves where they also accumulate. Here, we used a label free quantitative mass spectrometry approach to define the LD proteome of aging Arabidopsis leaves. We found that its composition is highly different from that of seed/cotyledon and identified 28 proteins including 9 enzymes of the secondary metabolism pathways involved in plant defense response. With the exception of the TRIGALACTOSYLDIACYLGLYCEROL2 protein, we did not identify enzymes implicated in lipid metabolism, suggesting that growth of leaf LDs does not occur by local lipid synthesis but rather through contact sites with the endoplasmic reticulum (ER) or other membranes. The two most abundant proteins of the leaf LDs are the CALEOSIN3 and the SMALL RUBBER PARTICLE1 (AtSRP1); both proteins have structural functions and participate in plant response to stress. CALEOSIN3 and AtSRP1 are part of larger protein families, yet no other members were enriched in the LD proteome suggesting a specific role of both proteins in aging leaves. We thus examined the function of AtSRP1 at this developmental stage and found that AtSRP1 modulates the expression of CALEOSIN3 in aging leaves. Furthermore, AtSRP1 overexpression induces the accumulation of triacylglycerol with an unusual composition compared to wild-type. We demonstrate that, although AtSRP1 expression is naturally increased in wild type senescing leaves, its overexpression in senescent transgenic lines induces an over-accumulation of LDs organized in clusters at restricted sites of the ER. Conversely, atsrp1 knock-down mutants displayed fewer but larger LDs. Together our results reveal that the abundancy of AtSRP1 regulates the neo-formation of LDs during senescence. Using electron tomography, we further provide evidence that LDs in leaves share tenuous physical continuity as well as numerous contact sites with the ER membrane. Thus, our data suggest that leaf LDs are functionally distinct from seed LDs and that their biogenesis is strictly controlled by AtSRP1 at restricted sites of the ER.

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StRemorin1.3 hampers Potato virus X TGBp1 ability to increase plasmodesmata permeability, but does not interfere with its silencing suppressor activity

Cited by 56 publications

References 37 publications

Plant immune and growth receptors share common signalling components but localise to distinct plasma membrane nanodomains

Plant immune and growth receptors share common signalling components but localise to distinct plasma membrane nanodomains

Lipid Raft, Regulator of Plasmodesmal Callose Homeostasis

Proteomic Analysis of Lipid Droplets from Arabidopsis Aging Leaves Brings New Insight into Their Biogenesis and Functions

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