Synaptotagmin SYTA Forms ER-Plasma Membrane Junctions that Are Recruited to Plasmodesmata for Plant Virus Movement

Levy, Amit; Zheng, Judy Y.; Lazarowitz, Sondra G.

doi:10.1016/j.cub.2015.06.015

Cited by 141 publications

(175 citation statements)

References 30 publications

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“…1B, C). This observation is in agreement with previous studies (Levy et al , 2015; Perez Sancho et al , 2015) and immunogold labeling of endogenous proteins (discussed later).…”

Section: Resultssupporting

confidence: 94%

“…Arabidopsis SYT1 is constitutively expressed in all tissues, and the mutants are more sensitive to salt, freezing, and mechanical stresses (Schapire et al , 2008; Yamazaki et al , 2008, 2010; Levy et al , 2015; Perez-Sancho et al , 2015). In addition, virus infections are delayed in SYT1 null mutants (Lewis and Lazarowitz, 2010; Uchiyama et al , 2014).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Arabidopsis SYT1 maintains stability of cortical endoplasmic reticulum networks and VAP27-1-enriched endoplasmic reticulum–plasma membrane contact sites

Siao

Wang

Voigt

et al. 2016

EXBOTJ

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“…1B, C). This observation is in agreement with previous studies (Levy et al , 2015; Perez Sancho et al , 2015) and immunogold labeling of endogenous proteins (discussed later).…”

Section: Resultssupporting

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Arabidopsis SYT1 maintains stability of cortical endoplasmic reticulum networks and VAP27-1-enriched endoplasmic reticulum–plasma membrane contact sites

Siao

Wang

Voigt

et al. 2016

EXBOTJ

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“…The ER also is attached to the PM through ER-PM contact sites (EPCSs), which are largely immotile subdomains of the ER that underlie the PM and whose number and density at the cell cortex diminish as cells expand (McFarlane et al, 2017). Fusion profiles of the ER membrane with the PM at the EPCSs have not been observed; however, proteins such as VAP27 proteins and Synaptotagmin1 (SYT1) have been shown to accumulate at the EPCSs Levy et al, 2015;Pérez-Sancho et al, 2015;Siao et al, 2016;McFarlane et al, 2017). The VAP proteins are conserved across kingdoms and possess three main regions, a C-terminal transmembrane domain, an N-terminal major sperm domain, and a coiled-coil domain .…”

Section: The Er Is a Pleomorphic Organelle Whose Morphology And Dynammentioning

confidence: 99%

Advances in Plant ER Architecture and Dynamics

Stefano

Brandizzí

2017

Plant Physiol.

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“…the remorin proteins REMORIN1.2 (REM1.2) and REM1.3 (Borner et al, 2005;Marín et al, 2012). A recent study (Levy et al, 2015) demonstrated that SYTA forms ER-PM junctions that are specifically recruited to PD during virus movement. Thus, proteins associated with the ER-PM contacts may be the specific targets of MPs during cell-to-cell movement.…”

Section: Validation Of the Proteomics Approachmentioning

confidence: 99%

“…Thus, proteins associated with the ER-PM contacts may be the specific targets of MPs during cell-to-cell movement. The association of these proteins with PD may provide a mechanism for targeting and concentrating viral genomes assembled on the actin-ER network and subsequently recruited to the entrances of PD (Tilsner et al, 2013;Levy et al, 2015). The PM intrinsic protein, PIP3, functions as an aquaporin and is induced by salt stress (Hachez et al, 2014b).…”

Section: Validation Of the Proteomics Approachmentioning

confidence: 99%

Reticulomics: Protein-protein interaction studies with two plasmodesmata-localised reticulon family proteins identify binding partners enriched at plasmodesmata, ER and the plasma membrane

et al. 2015

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The endoplasmic reticulum (ER) is a ubiquitous organelle that plays roles in secretory protein production, folding, quality control, and lipid biosynthesis. The cortical ER in plants is pleomorphic and structured as a tubular network capable of morphing into flat cisternae, mainly at three-way junctions, and back to tubules. Plant reticulon family proteins (RTNLB) tubulate the ER by dimerization and oligomerization, creating localized ER membrane tensions that result in membrane curvature. Some RTNLB ER-shaping proteins are present in the plasmodesmata (PD) proteome and may contribute to the formation of the desmotubule, the axial ER-derived structure that traverses primary PD. Here, we investigate the binding partners of two PD-resident reticulon proteins, RTNLB3 and RTNLB6, that are located in primary PD at cytokinesis in tobacco (Nicotiana tabacum). Coimmunoprecipitation of green fluorescent protein-tagged RTNLB3 and RTNLB6 followed by mass spectrometry detected a high percentage of known PD-localized proteins as well as plasma membrane proteins with putative membrane-anchoring roles. Förster resonance energy transfer by fluorescence lifetime imaging microscopy assays revealed a highly significant interaction of the detected PD proteins with the bait RTNLB proteins. Our data suggest that RTNLB proteins, in addition to a role in ER modeling, may play important roles in linking the cortical ER to the plasma membrane.The endoplasmic reticulum (ER) is a multifunctional organelle and is the site of secretory protein production, folding, and quality control (Brandizzi et al., 2003) and lipid biosynthesis (Wallis and Browse, 2010), but it is also involved in many other aspects of day-to-day plant life, including auxin regulation (Friml and Jones, 2010) and oil and protein body formation (Huang, 1996;Herman, 2008). The cortical ER network displays a remarkable polygonal arrangement of motile tubules that are capable of morphing into small cisternae, mainly at the three-way junctions of the ER network (Sparkes et al., 2009). The cortical ER network of plants has been shown to play multiple roles in protein trafficking (Palade, 1975;Vitale and Denecke, 1999) and pathogen responses (for review, see Pattison and Amtmann, 2009;Beck et al., 2012).In plants, the protein family of reticulons (RTNLBs) contributes significantly to tubulation of the ER (Tolley et al., 2008Chen et al., 2012). RTNLBs are integral ER membrane proteins that feature a C-terminal reticulon homology domain (RHD) that contains two major hydrophobic regions. These regions form two V-shaped transmembrane wedges joined together via a cytosolic loop, with the C and N termini of the protein facing the cytosol. RTNLBs can dimerize or oligomerize, creating localized tensions in the ER membrane, inducing varying degrees of membrane curvature . Hence, RTNLBs are considered to be essential in maintaining the tubular ER network.The ability of RTNLBs to constrict membranes is of interest in the context of cell plate development and the formation of primary plasmo...

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Synaptotagmin SYTA Forms ER-Plasma Membrane Junctions that Are Recruited to Plasmodesmata for Plant Virus Movement

Cited by 141 publications

References 30 publications

Arabidopsis SYT1 maintains stability of cortical endoplasmic reticulum networks and VAP27-1-enriched endoplasmic reticulum–plasma membrane contact sites

Arabidopsis SYT1 maintains stability of cortical endoplasmic reticulum networks and VAP27-1-enriched endoplasmic reticulum–plasma membrane contact sites

Advances in Plant ER Architecture and Dynamics

Reticulomics: Protein-protein interaction studies with two plasmodesmata-localised reticulon family proteins identify binding partners enriched at plasmodesmata, ER and the plasma membrane

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