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Plant Physiology Preview Published on February 13, 2009; 10.1104/pp.108.133827
OPEN ACCESS ARTICLE
Received December 5, 2008 Inhibition of TMV movement by expression of an actin-binding protein
Institut de Biologie Moleculaire des Plantes, Laboratoire propre du CNRS (UPR 2357) conventionne avec l'Universite Louis Pasteur (Strasbourg 1), 12 rue du General Zimmer, 67084 Strasbourg CEDEX, France; Laboratory of Plant Molecular Biology, CRP-Sante, 84 Val Fleuri, L-1526 Luxembourg * Corresponding author; email: manfred.heinlein{at}ibmp-ulp.u-strasbg.fr.
The TMV movement protein (MP) required for the cell-to-cell spread of viral RNA interacts with the ER as well as with the cytoskeleton during infection. Whereas associations of MP with ER and microtubules have been intensely investigated, research on the role of actin has been rather scarce. We demonstrate that Nicotiana benthamiana plants transgenic for the actin-binding protein ABD2:GFP exhibit a dynamic ABD2:GFP-labeled actin cytoskeleton and myosin-dependent Golgi trafficking. These plants also support the movement of TMV. In contrast, both myosin-dependent Golgi trafficking and TMV movement are dominantly inhibited when ABD2:GFP is expressed transiently. Inhibition is mediated through binding of ABD2:GFP to actin filaments since TMV movement is restored upon disruption of the ABD2:GFP-labeled actin network with Latrunculin B (LatB). LatB shows no significant effect on the spread of TMV infection in either wild type plants or ABD2:GFP-transgenic plants under our treatment conditions. We did not observe any binding of MP along the length of actin filaments. Collectively, these observations demonstrate that TMV movement does not require an intact actomyosin system. Nevertheless, actin binding proteins appear to have the potential to exert control over TMV movement through inhibition of myosin-associated protein trafficking along the ER membrane.
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