Professor Bernard L. Epel
Ph.D.: University of California, San Diego, USA, 1969
Phone: (Office) +972-3-640- 8598
(Home) +972- 9-950-3111
E-mail: blepel@post.tau.ac.il
Room#: Britannia 626
Member's portrait

Research Interests
 

The isolation and characterization of Pd proteins using proteomic techniques.
• The cloning and sequencing of genes to all Pd proteins.
• A functional and molecular characterization of Arabidopsis Pd mutants.
• The characterization of changes in the Pd composition in tissues undergoing developmental changes.
• The molecular characterization of Pd proteins associated with each type of Pd
• The identification of Pd proteins involved in virus MP and Pd interactions.
• The characterization at the biochemical and molecular level of changes in Pd composition resulting from MP expression in transgenic leaves expressing MP:GFP.
• The development of techniques to allow us to identify Pd protein involved in protein-protein interactions between Pd associated proteins and host-proteins that transport through or interact with Pd.


Selected Publications

Epel BL , Padgett HS, Heinlein M and Beachy RN (1996). Plant virus movement protein dynamics probed with a movement protein fused to GFP. Gene 173:75-79.

Fenczik CS., Epel BL and Beachy RN (1996). Role of plasmodesmata and viral movement protein in spread of plant viruses. In-: Plant Gene Research : Signal Transduction in Plant Development. Springer-Verlag, Wein, New York pp 249-279.

Padgett HS, Epel BL, Kahn TW, Heinlein M, Watanabe Y and Beachy RN (1996). Distribution of tobamovirus movement protein in infected cells and implications for cell-to-cell spread of infection. The Plant Journal 10:1079-1088.

Yahalom A, Lando R, Katz A and Epel BL (1998). A calcium-dependent protein kinase is associated with maize mesocotyl plasmodesmata. J Plant Physiol . 153:354-362.

Heinlein M, Padgett HS, Gens JS, Pickard BG, Casper SJ, Epel BL , and Beachy RN (1998). Changing patterns of localization of the tobacco mosaic virus movement protein and replicase to the endoplasmic reticulum and microtubules during infection. Plant Cell 10:1107-1120.

Oparka KJ, Roberts AG, Boevink P, Santa Cruz S, Roberts I, Pradel KS, Imlau A, Sauer N, Kotlizky G and Epel B (1999). Simple, but not branched, plasmodesmata allow the non-specific trafficking of proteins in developing tobacco leaves. Cell: 97: 743-754.

Kotlizky G, Boulton MI, Pitaksutheepong C, Davies JW and Epel BL (2000). Intracellular and intercellular movement of maize streak geminivirus V1 and V2 proteins transiently expressed as green fluorescent protein fusions. Virology. 274:32-38

Aaziz R, Dinant S and Epel BL (2001). Plasmodesmata and plant cytoskeleton. Trends Plant Sci. 6: 326-307

Kotlizky G, Katz A, van der Laak J, Boyko V, Lapidot M, Beachy RN, Heinlein M and Epel BL.(2001) A dysfunctional movement protein of tobacco mosaic virus interferes with targeting of wild-type movement protein to microtubules. Mol Plant Microbe Interact.14: 895-904

Gafni Y and Epel BL (2002). The role of host and viral proteins in intra- and inter-cellular trafficking of geminiviruses. Physiol Mol Plant Path. 60: 231-241

Man M and Epel BL (2004) Characterization of regulatory elements within the coat protein (CP) coding region of Tobacco mosaic virus affecting subgenomic transcription and green fluorescent protein expression from the CP subgenomic RNA promoter. J Gen Virol. 85:1727-1738

Heinlein M. and Epel BL (2004) (Invited review). Macromolecular transport and signaling through plasmodesmata. Int Rev Cytol. 2004;235:93-164.

Liarzi O. and Epel BL. (2005). The development of a quantitative tool for measuring changes in the coefficient of conductivity of plasmodesmata induced by developmental, biotic and abiotic signals. Protoplasma 225: 67-76.

Sagi G, Katz A, Guenoune-Gelbart D, and Epel BL (2005). Class 1 Reversibly Glycosylated Polypeptides Are Plasmodesmal-Associated Proteins Delivered to Plasmodesmata via the Golgi Apparatus. Plant Cell 17: 1788-1800.


My Theme
Plasmodesmata (Pd) are specialized gatable membranous trans-wall tunnels that interconnect the cytoplasm of contiguous cells and function in a direct intercellular movement of water, nutrients, small signaling molecules and, in certain cases, of macromolecules. The regulation of Pd conductance is under developmental control and may play an important function in the regulation of plant growth, development and morphogenesis. Plant viruses modify and exploit Pd as conduits for spreading from cell to cell.
Evidence is also accumulating that Pd can be gated and that Pd SEL can be modulated by environmental and developmental signals. Indirect data suggest Pd gating may be regulated by a phosphorylation /dephosphorylation mechanism.
Recent studies have demonstrated that Pd can also mediate cell-to-cell trafficking of macromolecules. These and other data lead to the concept that intercellular protein trafficking through Pd may functions in part in regulating plant development, physiology and responses to pathogens and environmental signals.
A fuller understanding of Pd function and regulation is dependent on the isolation and functional characterization of Pd components. Characterization of plasmodesmal associated proteins (PAPs) has been made possible by the development of techniques for isolation of clean wall fractions enriched in Pd and by the development by the Epel lab of techniques for isolating Pd.
What we do:
Professor Epel's group has pioneered in the assessment of Pd composition and has developed techniques for isolating Pd and for identifying Pd components. Furthermore, we and our collaborators are intensely involved in the exploration of virus (MP)-host interactions. A new and very exciting extension of these studies is the finding that Pd conductivity is under developmental control. The basic systematic approach of our lab of isolating and characterizing components of Pd is essential to an understanding of Pd functioning and regulation. This approach will facilitate the isolations of other cellular components involved in targeting to Pd and will provide the tools necessary to identify the facultative components that provide Pd with selectivity, tissue specificity etc.

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