Prof. Sagi-Eisenberg Ronit

  
Affiliation:Cell And Developmental Biology, Sackler School of Medicine
Tel:  (972)-3-6409500
 
Fax: (972)-3-6407432
 
Email: histol3@tau.ac.il
 
Personal Website:

 
Postal Address:Cell and Developmental Biology
Sackler School of Medicine

Tel Aviv University
Tel Aviv 69978

Research Interest

Nano scale functional genomics and proteomics analyses of mast cell activation
Allergic diseases including allergic rhinitis and conjunctivitis, urticaria, food allergy and asthma have reached epidemic proportions affecting more than 30% of the world population. Mast cells are central players in mediating allergic responses. Moreover, rapidly accumulating data clearly indicate implicate mast cells as major participants in chronic inflammatory diseases and autoimmune diseases. However, mast cells do also play a beneficial role in innate and adaptive immunity during bacteria infections. Thus, given the pleiotropic function of mast cells and their involvement in many major diseases, it is of great importance to elucidate the machineries and molecular mechanisms associated with mast cells activation. Thus, it is the focus of our research to decipher the molecular signaling networks linked with mast cell activation. Towards this end, we have taken three experimental approaches. The first approach involves a nano scale functional genomics high-throughput analyses of mast cell activation. Specifically, this approach involves the transfection of mast cells with GFP-tagged mutant protein cDNAs, alongside RFP-tagged reporters for mast cell activation. Both single cell and average readout image analyses are then performed and the data recapitulated in models that correlate the dynamics of cellular proteins with the state of activation. The second complementary approach follows specifically, the dynamics of selected essential proteins. Particularly, we correlate ERK activation with its nano-scale organization. Finally, our third approach involves the production of cell permeable peptides directed against intracellular targets. ALL1 is such peptide that targets the G-protein Gi3. Notably, this peptide, which displays remarkable inhibitory activity against mast cells both in vitro and in vivo self-assembles to form nano structures. Whether these structures contribute or rather reduce the activity of ALL1 is currently under investigation. 


Selected Publications


  • Melnikov S. and Sagi-Eisenberg, R.” Down-Regulating Protein Kinase C alpha: Functional Cooperation between the Proteasome and the Endocytic System”. Cell Signal. 21,1607-1619 (2009).
  • Shefler, I., Zavaro, O., Raz, T. Baram, D. and Sagi-Eisenberg, R. “Inhibition of basic secretagogues-induced signaling in mast cells by cell permeable Gαi -derived peptides.” Int. Arch. Allergy. 145,131-140 (2008).
  • Haberman, Y., Ziv, I., Gorzalczany, Y., Hirschberg, K., Mittleman, L., Fukuda, M. and Sagi-Eisenberg, R. “Synaptotagmin (Syt) IX is an essential determinant for protein sorting to secretory granules in mast cells”. Blood. 109, 3385-3392 (2007).
  • Kapp-Barnea, Y., Ninio-Many, L., Hirschberg, K., Fukuda, M., Jeromin, A. and Sagi-Eisenberg, R. “Neuronal Calcium Sensor-1 (NCS-1) and PI4Kβ stimulate ERK1/2 signaling by accelerating recycling through the endocytic recycling compartment (ERC).” MBC. 17, 4130-4141 (2006).