{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T01:47:08Z","timestamp":1790646428752,"version":"4.1.0"},"reference-count":82,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2021,1,25]],"date-time":"2021-01-25T00:00:00Z","timestamp":1611532800000},"content-version":"vor","delay-in-days":2224,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,1,26]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>The intercellular movement of plant viruses requires both viral and host proteins. Previous studies have demonstrated that the frame-shift protein P3N-PIPO (for the protein encoded by the open reading frame [ORF] containing 5\u2032-terminus of P3 and a +2 frame-shift ORF called Pretty Interesting Potyviridae ORF and embedded in the P3) and CYLINDRICAL INCLUSION (CI) proteins were required for potyvirus cell-to-cell movement. Here, we provide genetic evidence showing that a Tobacco vein banding mosaic virus (TVBMV; genus Potyvirus) mutant carrying a truncated PIPO domain of 58 amino acid residues could move between cells and induce systemic infection in Nicotiana benthamiana plants; mutants carrying a PIPO domain of seven, 20, or 43 amino acid residues failed to move between cells and cause systemic infection in this host plant. Interestingly, the movement-defective mutants produced progeny that eliminated the previously introduced stop codons and thus restored their systemic movement ability. We also present evidence showing that a developmentally regulated plasma membrane protein of N. benthamiana (referred to as NbDREPP) interacted with both P3N-PIPO and CI of the movement-competent TVBMV. The knockdown of NbDREPP gene expression in N. benthamiana impeded the cell-to-cell movement of TVBMV. NbDREPP was shown to colocalize with TVBMV P3N-PIPO and CI at plasmodesmata (PD) and traffic to PD via the early secretory pathway and the actomyosin motility system. We also show that myosin XI-2 is specially required for transporting NbDREPP to PD. In conclusion, NbDREPP is a key host protein within the early secretory pathway and the actomyosin motility system that interacts with two movement proteins and influences virus movement.<\/jats:p>","DOI":"10.1104\/pp.114.252734","type":"journal-article","created":{"date-parts":[[2014,12,25]],"date-time":"2014-12-25T05:46:30Z","timestamp":1419486390000},"page":"394-410","source":"Crossref","is-referenced-by-count":54,"title":["DEVELOPMENTALLY REGULATED PLASMA MEMBRANE PROTEIN of <i>Nicotiana benthamiana<\/i> Contributes to Potyvirus Movement and Transports to Plasmodesmata via the Early Secretory Pathway and the Actomyosin System\n\u00a0"],"prefix":"10.1093","volume":"167","author":[{"given":"Chao","family":"Geng","sequence":"first","affiliation":[{"name":"Laboratory of Plant Virology, Department of Plant Pathology, College of Plant Protection (C.G., Q.-Q.C., X.-D.L., A.-L.M., R.G., J.-L.L., Y.-P.T.), and"},{"name":"Collaborative Innovation Centre for Annually High Yield and High Efficiency Production of Wheat and Corn (C.G., X.-D.L.), Shandong Agricultural University, Tai\u2019an, Shandong 271018, China; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qian-Qian","family":"Cong","sequence":"additional","affiliation":[{"name":"Laboratory of Plant Virology, Department of Plant Pathology, College of Plant Protection (C.G., Q.-Q.C., X.-D.L., A.-L.M., R.G., J.-L.L., Y.-P.T.), and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiang-Dong","family":"Li","sequence":"additional","affiliation":[{"name":"Laboratory of Plant Virology, Department of Plant Pathology, College of Plant Protection (C.G., Q.-Q.C., X.-D.L., A.-L.M., R.G., J.-L.L., Y.-P.T.), and"},{"name":"Collaborative Innovation Centre for Annually High Yield and High Efficiency Production of Wheat and Corn (C.G., X.-D.L.), Shandong Agricultural University, Tai\u2019an, Shandong 271018, China; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"An-Li","family":"Mou","sequence":"additional","affiliation":[{"name":"Laboratory of Plant Virology, Department of Plant Pathology, College of Plant Protection (C.G., Q.-Q.C., X.-D.L., A.-L.M., R.G., J.-L.L., Y.-P.T.), and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rui","family":"Gao","sequence":"additional","affiliation":[{"name":"Laboratory of Plant Virology, Department of Plant Pathology, College of Plant Protection (C.G., Q.-Q.C., X.-D.L., A.-L.M., R.G., J.-L.L., Y.-P.T.), and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jin-Liang","family":"Liu","sequence":"additional","affiliation":[{"name":"Laboratory of Plant Virology, Department of Plant Pathology, College of Plant Protection (C.G., Q.-Q.C., X.-D.L., A.-L.M., R.G., J.-L.L., Y.-P.T.), and"},{"name":"College of Plant Sciences, Jilin University, Changchun 130062, China (J.-L.L.)"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan-Ping","family":"Tian","sequence":"additional","affiliation":[{"name":"Laboratory of Plant Virology, Department of Plant Pathology, College of Plant Protection (C.G., Q.-Q.C., X.-D.L., A.-L.M., R.G., J.-L.L., Y.-P.T.), and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2014,12,24]]},"reference":[{"key":"2021042014071141500_b1","doi-asserted-by":"crossref","first-page":"e1003683","DOI":"10.1371\/journal.ppat.1003683","article-title":"Contribution of host intracellular transport machineries to intercellular movement of turnip mosaic virus","volume":"9","author":"Agbeci","year":"2013","journal-title":"PLoS Pathog"},{"key":"2021042014071141500_b2","doi-asserted-by":"crossref","first-page":"e1001119","DOI":"10.1371\/journal.ppat.1001119","article-title":"A family of plasmodesmal proteins with receptor-like properties for plant viral movement 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