{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T23:31:11Z","timestamp":1792193471019,"version":"4.4.0"},"reference-count":58,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2022,8,20]],"date-time":"2022-08-20T00:00:00Z","timestamp":1660953600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100011310","name":"Rural and Environment Science and Analytical Services Division","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100011310","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012095","name":"Scottish Government","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012095","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/M007200\/1"],"award-info":[{"award-number":["BB\/M007200\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000271","name":"Science and Technology Facilities Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000271","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["bsppjournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Plant Pathology"],"published-print":{"date-parts":[[2022,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Plant reticulon (RTN) proteins are capable of constricting membranes and are vital for creating and maintaining tubules in the endoplasmic reticulum (ER), making them prime candidates for the formation of the desmotubule in plasmodesmata (PD). RTN3 and RTN6 have previously been detected in an\n                    <jats:italic>Arabidopsis<\/jats:italic>\n                    PD proteome and have been shown to be present in primary PD at cytokinesis. It has been suggested that RTN proteins form protein complexes with proteins in the PD plasma membrane and desmotubule to stabilize the desmotubule constriction and regulate PD aperture. Viral movement proteins (vMPs) enable the transport of viruses through PD and can be ER\u2010integral membrane proteins or interact with the ER. Some vMPs can themselves constrict ER membranes or localize to RTN\u2010containing tubules; RTN proteins and vMPs could be functionally linked or potentially interact. Here we show that different vMPs are capable of interacting with RTN3 and RTN6 in a membrane yeast two\u2010hybrid assay, coimmunoprecipitation, and F\u00f6rster resonance energy transfer measured by donor excited\u2010state fluorescence lifetime imaging microscopy. Furthermore, coexpression of the vMP CMV\u20103a and RTN3 results in either the vMP or the RTN changing subcellular localization and reduces the ability of CMV\u20103a to open PD, further indicating interactions between the two proteins.\n                  <\/jats:p>","DOI":"10.1111\/mpp.13261","type":"journal-article","created":{"date-parts":[[2022,8,20]],"date-time":"2022-08-20T22:54:46Z","timestamp":1661036086000},"page":"1807-1814","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Reticulons 3 and 6 interact with viral movement proteins"],"prefix":"10.1111","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3873-0650","authenticated-orcid":false,"given":"Jens","family":"Tilsner","sequence":"first","affiliation":[{"name":"Biomedical Sciences Research Complex School of Biology, Willie Russell Laboratories  Fife UK"},{"name":"Cell &amp; Molecular Sciences The James Hutton Institute  Dundee UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3782-5834","authenticated-orcid":false,"given":"Verena","family":"Kriechbaumer","sequence":"additional","affiliation":[{"name":"Endomembrane Structure and Function Research Group, Department of Biological and Medical Sciences Oxford Brookes University  Oxford 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