Recommend Plant Signaling & Behavior (PS&B) to your librarian for 2008. Download form here.

Sign up for Table of Contents Alerts!

home subscribe search archive forthcoming

PS&B is the official journal of the Society for Plant Neurobiology. Full membership ($60 annually) and student membership ($30 annually) include online access to the journal. Click here to join.

Email this page Print this page

Article Addendum

β-1,3-Glucanases: Plasmodesmal Gate Keepers for Intercellular Communication

Amit Levy, Dana Guenoune-Gelbart and Bernard L. Epel

volume 2 | issue 5

september/october
Pages: 404 - 406

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.

Plasmodesmata (Pd), coaxial membranous channels that connect adjacent plant cells, are not static, but show a dynamic nature and can be opened or closed. These controlled changes in Pd conductivity regulate plant symplasmic permeability and play a role both in development and defense processes. One of the mechanisms shown to produce these changes is the deposition and hydrolysis of callose by β-1-3-synthase and glucanase, respectively. Recently we have identified the first β-1,3-glucanase Arabidopsis enzyme that is associated to the macromolecular Pd complex, termed AtBG_pap. When fused to GFP, this previously identified GPI-anchored protein localizes to the ER and the plasma membrane where it appears in a punctuate pattern that co-localizes with callose present around Pd. In T-DNA insertion mutants that do not transcribe AtBG_pap, GFP cell-to-cell movement between epidermal cells is reduced and callose levels around Pd are elevated. In this addenda we review the plant developmental processes of symplasmic regulation that have been shown to include callose deposition and β-1,3-glucanase activity, and suggest a role for AtBG_pap in these processes. Additionally, based on the ability of viral movement proteins (MPs) to interact with ankyrin repeat proteins, and together with our recent findings showing the involvement of viral particles in callose degradation, we also purpose a new model for the ability of viruses to overcome Pd-callose deposition, and mediate their cell-to-cell movement.

Authors

Amit Levy

Tel Aviv University, Tel Aviv, Israel

Dana Guenoune-Gelbart

Tel Aviv University, Tel Aviv, Israel

Bernard L. Epel

Tel Aviv University, Tel Aviv, Israel



We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.