Novel Aquaporin Regulatory Mechanisms Revealed by Interactomics

Bellati, Jorge; Champeyroux, Chloé; Hem, Sonia; Rofidal, Valérie; Krouk, Gabriel; Maurel, Christophe; Santoni, Véronique

doi:10.1074/mcp.m116.060087

Cited by 77 publications

(89 citation statements)

References 90 publications

(105 reference statements)

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“…We also identified aquaporin PIP3 (AT4G35100), 283 which is a homolog of RGS1-associated protein, PIP2;1 . Interestingly, 284 aquaporins are also associated with FER, which regulates the permeability of water channels 285 through modulating phosphorylation status of aquaporins (Bellati et al, 2016). Moreover, the 286 auxin transporter PIN3 (AT1G70940) and a defense related protein NDR/HIN1-LIKE 3 287 (AT5G06320) found in this study (Table 1) may be related to G-protein-mediated auxin (Ullah et 288 al., 2003;Mudgil et al, 2009) and defense responses (Llorente et al, 2005;Zhu et al, 2009;289 Liang et al, 2016).…”

Section: Co-ip Provides New Insights On the G Protein Interactome 265mentioning

confidence: 89%

The G Protein β-Subunit, AGB1, Interacts with FERONIA in RALF1-Regulated Stomatal Movement

Chakravorty

Assmann

2018

Plant Physiol.

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Section: Co-ip Provides New Insights On the G Protein Interactome 265mentioning

confidence: 89%

The G Protein β-Subunit, AGB1, Interacts with FERONIA in RALF1-Regulated Stomatal Movement

Chakravorty

Assmann

2018

Plant Physiol.

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“…Downregulated PIP2 may break the interaction with PIP1 and reduce water uptake leading to the switch into Phase II of seed germination. Additionally, PIP2s also interact with vesicle trafficking syntaxins (Hachez et al , ; Bellati et al , ). V‐ATPase coupled with ATP hydrolysis across the tonoplast serves as a central regulator of intracellular ion homeostasis and vacuolar/cytoplasmic pH.…”

Section: Discussionmentioning

confidence: 99%

Quantitative ubiquitylomics approach for characterizing the dynamic change and extensive modulation of ubiquitylation in rice seed germination

Damaris

et al. 2019

The Plant Journal

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Summary During seed germination, cells embark on extensive post‐transcriptional and post‐translational modifications (PTM), providing a perfect platform to study these events in embryo rebooting from relative quiescenct to highly active state. PR‐619, a deubiquitylase inhibitor, delayed the rice seed germination and resulted in the accumulation of ubiquitylated proteins, which indicated the protein ubiquitylation is involved in this process. Using the K‐Ɛ‐GG antibody enrichment method integrated with high‐resolution mass spectrometry, a list of 2576 lysine ubiquitylated (Kub) sites in 1171 proteins was compiled for rice embryos at 0, 12 and 24 h after imbibition (HAI). Of these, the abundance of 1419 Kub sites in 777 proteins changed significantly. Most of them substantially increased within the first 12 HAI, which is similar to the dynamic state previously observed for protein phosphorylation, implying that the first 12 HAI are essential for subsequent switch during rice seed germination. We also quantitatively analyzed the embryo proteome in these samples. Generally, a specific protein’s abundance in the ubiquitylome was uncorrelated to that in the proteome. The differentially ubiquitinated proteins were greatly enriched in the categories of protein processing, DNA and RNA processing/regulation related, signaling, and transport. The DiGly footprint of the Kub sites was significantly reduced on K48, a linkage typically associated with proteasome‐mediated degradation. These observations suggest ubiquitylation may modulate the protein function more than providing 26S degradation signals in the early stage of rice seed germination. Revealing this comprehensive ubiquitylome greatly increases our understanding of this critical PTM during seed germination.

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“…In addition, several proteins specific to TG and showing higher total score (sum of the scores of all peptide matches) than GFP were also identified (Table S1). Among them, AT3G16470 was reported as a GFP-interacting protein (Bellati et al 2016). Meanwhile, there was no overlap with proteins that interacted with AtPIP2;1 (BioGRID Database for PIP2;1, https://thebiogrid.org/) (Bellati et al 2016).…”

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confidence: 99%

“…Among them, AT3G16470 was reported as a GFP-interacting protein (Bellati et al 2016). Meanwhile, there was no overlap with proteins that interacted with AtPIP2;1 (BioGRID Database for PIP2;1, https://thebiogrid.org/) (Bellati et al 2016). Therefore, it was suggested that these proteins were isolated because of artificial binding to GFP or AtPIP2;1 during the experiment.…”

mentioning

confidence: 99%

“…As the immunoprecipitation of GFP-tagged nucleoporin also enabled the identification of proteins forming the nucleoporin complex (Tamura et al 2010), we expected that proteins binding to the targeted egg cell plasma membrane protein would be isolable by our method. In addition, it was reported that cross-link of protein complexes by formaldehyde treatment allowed isolation of many AtPIP2;1 interacting membrane proteins from whole plants expressing 35Spro::GFP-AtPIP2;1 (Bellati et al 2016). Application of the known male fertilization regulators such as GCS1/HAP2 and GEX2 fused to Figure 1B.…”

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confidence: 99%

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Isolation of GFP-tagged plasma membrane protein from Arabidopsis egg cells

Igawa

Yamada

Sawada

et al. 2017

Plant Biotechnology

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Angiosperms possess a double fertilization system for sexual reproduction. Double fertilization is regulated by interactions among proteins localized in the plasma membrane of each sex gamete. A few plasma membrane resident proteins regulating double fertilization have been identified in male gametes. In contrast, no fertilization regulators in female gamete plasma membrane have been identified, largely due to difficulties in the isolation and collection of female gametes. We had produced Arabidopsis transgenic plant pDD45::GFP-AtPIP2;1 where the egg cell plasma membrane was specifically labeled with GFP ). The protein extract derived from approximately 200 pistils, which contained unfertilized and mature egg cells, was subjected to immunoprecipitation using anti-GFP antibody. As a result, both GFP and AtPIP2;1 were specifically detected in immunoprecipitated proteins from pistil tissues of pDD45::GFP-AtPIP2;1 transgenic plant, but not in those of wild type pistils. It was revealed that specific proteins expressed in the egg cells were successfully isolated from pistil cell population. The method described here showed the feasibility of isolating specific egg cell plasma membrane protein without gamete isolation and collection procedures.

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Novel Aquaporin Regulatory Mechanisms Revealed by Interactomics

Cited by 77 publications

References 90 publications

The G Protein β-Subunit, AGB1, Interacts with FERONIA in RALF1-Regulated Stomatal Movement

The G Protein β-Subunit, AGB1, Interacts with FERONIA in RALF1-Regulated Stomatal Movement

Quantitative ubiquitylomics approach for characterizing the dynamic change and extensive modulation of ubiquitylation in rice seed germination

Isolation of GFP-tagged plasma membrane protein from Arabidopsis egg cells

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