Targeting of TMV movement protein to plasmodesmata requires the actin/ER network: evidence from FRAP

Kathryn M. Wright, Nicola T. Wood, Alison G. Roberts, Sean Chapman, Petra Boevink, Katrin M. MacKenzie, Karl J. Oparka

    Research output: Contribution to journalArticlepeer-review

    124 Citations (Scopus)


    Fluorescence recovery after photobleaching (FRAP) was used to study the mechanism by which fluorescent-protein-tagged movement protein (MP) of tobacco mosaic virus (TMV) is targeted to plasmodesmata (PD). The data show that fluorescence recovery in PD at the leading edge of an infection requires elements of the cortical actin/endoplasmic reticulum (ER) network and can occur in the absence of an intact microtubule (MT) cytoskeleton. Inhibitors of the actin cytoskeleton (latrunculin and cytochalasin) significantly inhibited MP targeting, while MT inhibitors (colchicine and oryzalin) did not. Application of sodium azide to infected cells implicated an active component of MP transfer to PD. Treatment of cells with Brefeldin A (BFA) at a concentration that caused reabsorption of the Golgi bodies into the ER (precluding secretion of viral MP) had no effect on MP targeting, while disruption of the cortical ER with higher concentrations of BFA caused significant inhibition. Our results support a model of TMV MP function in which targeting of MP to PD during infection is mediated by the actin/ER network.
    Original languageEnglish
    Pages (from-to)21-31
    Number of pages11
    Issue number1
    Publication statusPublished - Jan 2007


    • Actins
    • Bicyclo Compounds, Heterocyclic
    • Biological Transport, Active
    • Brefeldin A
    • Cytochalasin B
    • Endoplasmic Reticulum
    • Fluorescence Recovery After Photobleaching
    • Microtubules
    • Plant Viral Movement Proteins
    • Plants, Genetically Modified
    • Plasmodesmata
    • Sodium Azide
    • Thiazolidines
    • Tobacco
    • Tobacco Mosaic Virus


    Dive into the research topics of 'Targeting of TMV movement protein to plasmodesmata requires the actin/ER network: evidence from FRAP'. Together they form a unique fingerprint.

    Cite this