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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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Kriechbaumer, Verena, Botchway, Stanley W., Slade, Susan E., Knox, Kirsten, Frigerio, Lorenzo, Oparka, Karl J. and Hawes, Chris (2015) Reticulomics : protein-protein interaction studies with two plasmodesmata-localised reticulon family proteins identify binding partners enriched at plasmodesmata, ER and the plasma membrane. Plant Physiology, 169 (3). pp. 1933-1945. doi:10.1104/pp.15.01153

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Official URL: http://dx.doi.org/10.1104/pp.15.01153

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Abstract

The 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 (RTNLB) proteins tubulate the ER by dimer- and oligomerization, creating localised ER membrane tensions that result in membrane curvature. Some RTNLB ER-shaping proteins are present in the plasmodesmal (PD) proteome (Fernandez-Calvino et al., 2011) and may contribute to the formation of the desmotubule, the axial ER-derived structure that traverses primary PD (Knox et al., 2015). Here we investigate the binding partners of two PD-resident reticulon proteins, RTNLB3 and RTNLB6, that are located in primary PD at cytokinesis (Knox et al., 2015). Co-immunoprecipitation of GFP-tagged RTNLB3 and RTNLB6 followed by mass spectrometry detected a high percentage of known PD-localised proteins as well as plasma-membrane proteins with putative membrane anchoring roles. FRET-FLIM 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 modelling, may play important roles in linking the cortical ER to the plasma membrane.

Item Type: Journal Article
Divisions: Faculty of Science > Life Sciences (2010- )
Journal or Publication Title: Plant Physiology
Publisher: American Society of Plant Biologists
ISSN: 0032-0889
Official Date: November 2015
Dates:
DateEvent
November 2015Published
September 2015Available
8 September 2015Accepted
24 July 2015Submitted
Date of first compliant deposit: 31 December 2015
Volume: 169
Number: 3
Page Range: pp. 1933-1945
DOI: 10.1104/pp.15.01153
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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