Reticulons 3 and 6 interact with viral movement proteins
Abstract
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 Arabidopsis 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-integral membrane proteins or interact with the ER. Some vMPs can themselves constrict ER membranes or localize to RTN-containing 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-hybrid assay, coimmunoprecipitation, and Förster resonance energy transfer measured by donor excited-state fluorescence lifetime imaging microscopy. Furthermore, coexpression of the vMP CMV-3a and RTN3 results in either the vMP or the RTN changing subcellular localization and reduces the ability of CMV-3a to open PD, further indicating interactions between the two proteins.
Citation
Tilsner , J & Kriechbaumer , V 2022 , ' Reticulons 3 and 6 interact with viral movement proteins ' , Molecular Plant Pathology , vol. Early View . https://doi.org/10.1111/mpp.13261
Publication
Molecular Plant Pathology
Status
Peer reviewed
ISSN
1464-6722Type
Journal article
Description
Funding; This research was funded by the Science and Technology Facilities Council Programme (grant no. 14230008), a British Biotechnology and Biological Sciences Research Council (grant no. BB/J004987/1 to Professor Chris Hawes), and a Vice-Chancellors Research Fellowship to V.K. Parts of this work were funded by the U.K. Biotechnology and Biomedical Sciences Research Council (BBSRC) grant BB/M007200/1 to J.T. Work in J.T.'s laboratory is supported by the Scottish Government's Rural and Environment Science and Analytical Services Division (RESAS).Collections
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