Multiple C2 domains and Transmembrane region Proteins (MCTPs) tether membranes at plasmodesmata

Brault, Marie L; Petit, J.P.; Immel, Françoise; Nicolas, William J; Brocard, Lysiane; Gaston, Amélia; Fouché, Mathieu; Hawkins, Timothy J.; Crowet, Jean-Marc; Grison, Magali; Kraner, Max; Alva, Vikram; Claverol, Stéphane; Deleu, Magali; Lins, Laurence; Tilsner, Jens; Bayer, Emmanuelle

doi:10.1101/423905

Cited by 26 publications

(58 citation statements)

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“…PD are viewed as signalling hub (Lee, 2015) and special membrane contact sites (MCSs) (Tilsner & Torrance, 2011;P erez-Sancho et al, 2016;Tilsner et al, 2016;Bayer et al, 2017;Brault et al, 2019), with lipid rafts or nanodomains (NDs) enriched in sterol and sphingolipids resident on the PD-PM (Raffaele et al, 2009;Mongrand et al, 2010;Tilsner & Torrance, 2011;Grison et al, 2015;Yan et al, 2019). Several functional proteins and signalling lipids are recruited to these NDs by lateral segregation to regulate PD permeability.…”

Section: Discussionmentioning

confidence: 99%

Remorin interacting with PCaP1 impairs Turnip mosaic virus intercellular movement but is antagonised by VPg

et al. 2019

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Group 1 Remorins (REMs) are extensively involved in virus trafficking through plasmodesmata (PD). However, their roles in Potyvirus cell-to-cell movement are not known. The plasma membrane (PM)-associated Ca 2+ binding protein 1 (PCaP1) interacts with the P3N-PIPO of Turnip mosaic virus (TuMV) and is required for TuMV cell-to-cell movement, but the underlying mechanism remains elusive.The mutant plants with overexpression or knockout of REM1.2 were used to investigate its role in TuMV cell-to-cell movement. Arabidopsis thaliana complementary mutants of pcap1 were used to investigate the role of PCaP1 in TuMV cell-to-cell movement. Yeast-two-hybrid, bimolecular fluorescence complementation, co-immunoprecipitation and RT-qPCR assays were employed to investigate the underlying molecular mechanism.The results show that TuMV-P3N-PIPO recruits PCaP1 to PD and the actin filament-severing activity of PCaP1 is required for TuMV intercellular movement. REM1.2 negatively regulates the cell-to-cell movement of TuMV via competition with PCaP1 for binding actin filaments. As a counteractive response, TuMV mediates REM1.2 degradation via both 26S ubiquitin-proteasome and autophagy pathways through the interaction of VPg with REM1.2 to establish systemic infection in Arabidopsis.This work unveils the actin cytoskeleton and PM nanodomain-associated molecular events underlying the cell-to-cell movement of potyviruses.

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Section: Discussionmentioning

confidence: 99%

Remorin interacting with PCaP1 impairs Turnip mosaic virus intercellular movement but is antagonised by VPg

et al. 2019

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“…A survey of the recently published Arabidopsis plasmodesmata-proteome (Brault et al, 2019) identified several members of the RLK family present in the plasmodesmata fraction with clade III members being predominant (Supplemental Table S1). As plasmodesmata have been reported to be composed of sterol-and sphingolipid-enriched microdomains (Grison et al, 2015a; Nicolas et al, 2017), we focused on RLKs, which may preferentially associate with lipid microdomains by cross referencing the accessions with seven published detergent-resistant membrane (DRM) proteomes (Shahollari et al, 2004(Shahollari et al, , 2005Kierszniowska et al, 2009;Minami et al, 2009;Keinath et al, 2010;Demir et al, 2013;Srivastava et al, 2013;Szymanski et al, 2015).…”

Section: The Pm-associated Lrr-rlks Qsk1 and Imk2 Dynamically Associamentioning

confidence: 99%

“…We used the label-free plasmodesmata proteomic analysis of Brault et al (2019) to select RLK candidates. For that, all members of the LRR-RLK family that displayed with a significant fold change (plasmodesmata/PM enrichment ratio .…”

Section: Proteomic Analysesmentioning

confidence: 99%

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Plasma Membrane-Associated Receptor-like Kinases Relocalize to Plasmodesmata in Response to Osmotic Stress

et al. 2019

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Plasmodesmata act as key elements in intercellular communication, coordinating processes related to plant growth, development, and responses to environmental stresses. While many of the developmental, biotic, and abiotic signals are primarily perceived at the plasma membrane (PM) by receptor proteins, plasmodesmata also cluster receptor-like activities; whether these two pathways interact is currently unknown. Here, we show that specific PM-located Leu-rich-repeat receptor-like-kinases, Qi an Sh ou kinase (QSK1) and inflorescence meristem kinase2, which under optimal growth conditions are absent from plasmodesmata, rapidly relocate and cluster to the pores in response to osmotic stress. This process is remarkably fast, is not a general feature of PM-associated proteins, and is independent of sterol and sphingolipid membrane composition. Focusing on QSK1, previously reported to be involved in stress responses, we show that relocalization in response to mannitol depends on QSK1 phosphorylation. Loss-of-function mutation in QSK1 results in delayed lateral root (LR) development, and the mutant is affected in the root response to mannitol stress. Callosemediated plasmodesmata regulation is known to regulate LR development. We found that callose levels are reduced in the qsk1 mutant background with a root phenotype resembling ectopic expression of PdBG1, an enzyme that degrades callose at the pores. Both the LR and callose phenotypes can be complemented by expression of wild-type and phosphomimic QSK1 variants, but not by phosphodead QSK1 mutant, which fails to relocalize at plasmodesmata. Together, the data indicate that reorganization of receptor-like-kinases to plasmodesmata is important for the regulation of callose and LR development as part of the plant response to osmotic stress.

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“…One significant feature of the PD is a strand of endoplasmic reticulum (ER) that traverses the pore and is tethered tightly to the plasma membrane (PM) by unidentified spokes [5]. Recent study has demonstrated that multiple C2 domains and transmembrane region proteins (MCTPs) are core PD proteins involved in tethering ER and PM [6].…”

Section: Introductionmentioning

confidence: 99%

Genome-wide identification and characterization of multiple C2 domains and transmembrane region proteins in Gossypium hirsutum

Hao

Wang

et al. 2020

BMC Genomics

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Background: Multiple C2 domains and transmembrane region proteins (MCTPs) may act as transport mediators of other regulators. Although increased number of MCTPs in higher plants implies their diverse and specific functions in plant growth and development, only a few plant MCTPs have been studied and no study on the MCTPs in cotton has been reported. Results: In this study, we identified 31 MCTPs in G. hirsutum, which were classified into five subfamilies according to the phylogenetic analysis. GhMCTPs from subfamily V exhibited isoelectric points (pIs) less than 7, whereas GhMCTPs from subfamily I, II, III and IV exhibited pIs more than 7.5, implying their distinct biological functions. In addition, GhMCTPs within subfamily III, IV and V exhibited more diverse physicochemical properties, domain architectures and expression patterns than GhMCTPs within subfamily I and II, suggesting that GhMCTPs within subfamily III, IV and V diverged to perform more diverse and specific functions. Analyses of conserved motifs and pIs indicated that the N-terminus was more divergent than the C-terminus and GhMCTPs' functional divergence might be mainly contributed by the N-terminus. Furthermore, yeast two-hybrid assay indicated that the N-terminus was responsible to interact with target proteins. Phylogenetic analysis classified multiple N-terminal C2 domains into four subclades, suggesting that these C2 domains performed different molecular functions in mediating the transport of target proteins. Conclusions: Our systematic characterization of MCTPs in G. hirsutum will provide helpful information to further research GhMCTPs' molecular roles in mediating other regulators' transport to coordinate growth and development of various cotton tissues.

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Multiple C2 domains and Transmembrane region Proteins (MCTPs) tether membranes at plasmodesmata

Cited by 26 publications

References 100 publications

Remorin interacting with PCaP1 impairs Turnip mosaic virus intercellular movement but is antagonised by VPg

Remorin interacting with PCaP1 impairs Turnip mosaic virus intercellular movement but is antagonised by VPg

Plasma Membrane-Associated Receptor-like Kinases Relocalize to Plasmodesmata in Response to Osmotic Stress

Genome-wide identification and characterization of multiple C2 domains and transmembrane region proteins in Gossypium hirsutum

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