Bengal Eyal - Associate Professor
- Phone: 972-4-829-5287
- Email: firstname.lastname@example.org
- Office: Faculty of Medicine, 6th floor
- Fax: 972-4-855-3299
Hebrew University, 1982 B.Sc.
Weizmann Institute, 1985 M.Sc.
Weizmann Institute 1990 Ph.D.
Main Research Area
In mammals, it is well established that several factors secreted in the somite environment initiate the myogenic program that is characterized by the activation of two muscle regulatory factors (MRFs), Myf5 and MyoD. Although the MRFs are essential for the establishment of muscle cell precursors and their differentiation, little is known about the intracellular signals that activate their expression in the proper time and place during development. We have been investigating several signaling cascades, such as those of mitogen-activated protein kinases (MAPKs) and phosphatidylinositol 3-kinases (PI3-kinases), involved in cell growth and differentiation. We found these pathways are involved in different aspects of cell cycle, cell survival and differentiation in tissue culture models of myogenesis. Our goal is to understand the function of these pathways in muscle formation during embryo development and in the destruction of adult muscle tissue that occurs in muscular dystrophies and in chronic diseases leading to muscle cachexia. The role of these pathways during muscle development will be studied in the frog Xenopus laevis and their possible role in muscle disease will be investigated in mouse models.
A second topic being studied is early patterning in the frog Xenopus laevis. We have identified signaling pathways and transcription factors that function in the specification of different germ layers and the patterning of the embryo. These are being studied in great detail that will enable to decipher the earliest events in embryogenesis.
Overall, our studies should broaden our understanding of the principal mechanisms regulating patterning and normal development of skeletal muscles as well as their regeneration in disease and aging .
1. The role of Kirrel3 receptor in myoblast fusion.
2. Signaling pathways and transcription factors involved in germ layer specification and patterning of the frog embryo.
3. ER stress and skeletal muscle regeneration
Items 1 – 16
1: Keren-Politansky A, Keren A, Bengal E.
Neural ectoderm-secreted FGF initiates the expression of Nkx2.5 in cardiac progenitors via a p38 MAPK/CREB pathway.
Dev Biol. 01/11/2009; 2: 374 – 384
2: Keren A, Keren-Politansky A, Bengal E.
A p38 MAPK-CREB pathway functions to pattern mesoderm in Xenopus.
Dev Biol. 01/10/2008; 1: 86 – 94
3: Alter J, Rozentzweig D, Bengal E.
Inhibition of myoblast differentiation by tumor necrosis factor alpha is mediated by c-Jun N-terminal kinase 1 and leukemia inhibitory factor.
J Biol Chem. 01/01/2008; 34: 23224 – 23234
4: Penn, BH., Bergstrom, DA., Dilworth, FJ., Bengal, E., and Tapscott, SJ
A MyoD-generated feed-forward circuit temporally patterns gene expression during skeletal muscle differentiation.
Genes & Dev. 01/01/2004; 18: 2348 – 2353
5: Reuveny , M., Heller, H., and Bengal, E.
RhoA controls myoblast survival by inducing the phosphatidylinositol 3-kinase-Akt signaling pathway.
FEBS Letters 01/01/2004; 569: 129 – 134
6: Ostrovsky, O., and Bengal, E.
The Mitogen-activated protein kinase cascade promotes myoblast cell survival by stabilizing the cyclin-dependent kinase inhibitor, p21WAF1 protein.
J. Biol. Chem. 01/01/2003; 278: 21221 – 21231
7: Ostrovsky O., Bengal, E., and Aronheim, A.
Induction of Terminal Differentiation by the c-Jun Dimerization Protein JDP2 in C2 Myoblasts and Rhabdomyosarcoma Cells.
J. Biol. Chem. 01/01/2002; 277: 40043 – 40054
8: Zetser, A., Frank, D., and Bengal, E.
MAP kinase converts MyoD into an instructive muscle differentiation factor in Xenopus.
Dev. Biol. 01/01/2001; 240: 168 – 181
9: Heller, H., Gredinger, E and Bengal, E.
Rac1 inhibits myogenic differentiation by preventing the complete withdrawal of myoblasts from the cell cycle.
J. Biol. Chem. 01/01/2001; 276: 37307 – 37316
10: Tamir, Y., and Bengal E.
Phosphoinositide 3-kinase induces the transcriptional activity of MEF2 proteins during muscle differentiation.
J. Biol. Chem. 01/01/2000; 275: 34424 – 34432
11: Zetser, A., Gredinger, E., and Bengal, E.
p38 mitogen-activated protein kinase promotes skeletal muscle differentiation: participation of the MEF2C transcription factor.
J. Biol. Chem. 01/01/1999; 274: 5193 – 5200
12: Tamir, Y., and Bengal, E.
p53 protein is activated during muscle differentiation and participates with MyoD in the transcription of muscle creatine kinase gene.
Oncogene 01/01/1998; 17: 347 – 356
13: Abu-Hatoum, O., Gross-Mesilati, S., Breitschopf, K., Hoffman, A., Gonen, H., Ciechanover, A., and Bengal, E.
Degradation of the myogenic transcription factor MyoD by the ubiquitin pathway in vivo and in vitro: Regulation by specific DNA binding.
Mol. Cell. Biol. 01/01/1998; 18: 5670 – 5677
14: Heller, H., and Bengal, E.
TFIID (TBP) stabilizes the binding of MyoD to its DNA site at the promoter and MyoD facilitates the association of TFIIB with the preinitiation complex.
Nucl. Acids Res. 01/01/1998; 26: 2112 – 2119
15: Gredinger, E., Gerber, A.N., Tamir, Y., Tapscott S.J. and Bengal E.
Mitogen-activated protein kinase pathway is involved in the differentiation of muscle cells.
J. Biol. Chem 01/01/1998; 273: 10436 – 10444
16: Keren, A., Bengal, E.*, and Frank, D
p38 MAP Kinase Regulates the Expression of XMyf5 and Affects Distinct Myogenic Programs during Xenopus Development.
Dev. Biol. 2005 288: 73 – 86