Gloria Volohonsky

Gloria Volohonsky 

Post-doctoral Researcher

tel: (+33) 3 88 41 70 95
fax: (+33) 3 88 60 69 22

Send an email


2000-2005 : Ph.D, Biology. Research topic : Elucidating the molecular function of the Drosophila mRNA binding protein HOW. Thesis title : “The Molecular mechanism of Drosophila HOW proteins in controlling mRNA expression”. The Feinberg Graduate School, Weizmann Institute of Science, Rehovot, Israel.

2005-2006 : Post doctoral position. Research topic : Selection and maturation of muscle attachment cells – the role of an alternatively spliced transcription factor Stripe. Advisor : Prof. Talila Volk. Weizmann Institute of Science, Rehovot, Israel.

2007-2008 : Post doctoral position. Research topic : Illucidating the molecular mechanisms of glia chain cell migration. Advisor : Anglea Giangrande, IGBMC, Illkirch, France

in the lab between 2008 and 2014


17. Transgenic expression of the anti-parasitic factor TEP1 in the malaria mosquito Anopheles gambiae.  G Volohonsky, A-K Hopp, Mélanie Saenger, Julien Soichot, H Scholze, J Boch, Stéphanie Blandin, Eric Marois, 2017  – PLoS Pathog  13(1):e1006113 pubmed

16. Tools for Anopheles gambiae Transgenesis. Volohonsky G.*, Terenzi O.*, Soichot J.*, Naujoks D.A., Nolan T., Windbichler N., Kapps D., Smidler A.L., Vittu A., Costa G., Steinert S., Levashina E.A., Blandin S.A. and Marois E., 2015 – Genes, Genomes, Genetics 5(6):1151-63 pubmed

15. A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae. Baxter R.H., Steinert S., Chelliah Y., Volohonsky G., Levashina E.A., Deisenhofer J., 2010 – Proc. Natl. Acad. Sci. U S A. 107(39):16817-22 pubmed

14. Focusing on complement in the antiparasitic defense of mosquitoes. Volohonsky G., Steinert S., Levashina E.A., 2010 – Trends Parasitol.  26(1):1-3 pubmed

13. Post-transcriptional repression of the Drosophila midkine and pleiotrophin homolog miple by HOW is essential for correct mesoderm spreading. Toledano-Katchalski H., Nir R., Volohonsky G., Volk T., 2007 – Development 134:3473-81 pubmed

12. Muscle-dependent maturation of tendon cells is induced by post-transcriptional regulation of stripeA. Volohonsky G., Edenfeld G., Klambt C., Volk T., 2007 – Development 134:347-56 pubmed

11. The splicing factor crooked neck associates with the RNA-binding protein HOW to control glial cell maturation in Drosophila. Edenfeld G., Volohonsky G., et al., 2006 – Neuron 52:969-80 pubmed

10. EGFR signaling attenuates Groucho-dependent repression to antagonize Notch transcriptional output. Hasson P., Egoz N., Winkler C., Volohonsky G., Jia S., Dinur T., Volk T., Courey A.J., Paroush Z., 2005 – Nat Genet. 37(1):101-5 pubmed

9. Cell divisions in the Drosophila embryonic mesoderm are repressed via posttranscriptional regulation of string/cdc25 by HOW. Nabel-Rosen H., Toledano-Katchalski H., Volohonsky G., Volk T., 2005 – Curr Biol. 15(4):295-302 pubmed

8. Two isoforms of the Drosophila RNA-binding protein, How, act in opposing directions to regulate tendon cell differentiation. Nabel-Rosen H.*., Volohonsky G.*., Reuveny A., Zaidel-Bar R., and Volk T., 2002 – Develpmental Cell 2:183-193. *Equal contribution pubmed

7. Nuclear localization of non-receptor protein tyrosine phosphatase epsilon is regulated by its unique N-terminal domain. Kraut J., Volohonsky G., Toledano-Katchalski H., Elson A., 2002 – Exp Cell Res. 281(2):182-9. pubmed

6. Regulation of protein-tyrosine phosphatases alpha and epsilon by calpain-mediated proteolytic cleavage. Gil-Henn H., Volohonsky G., and Elson A., 2001 – J Biol Chem. 276:31772-9. pubmed

5. Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control. Gil-Henn H., Volohonsky G., Toledano-Katchalski H., Gandre S., and Elson A., 2000 – Oncogene 19:4375-84. pubmed

4. The role of gamma-glutamyl transpeptidase in the biosynthesis of glutathione. Stark A.A., Porat N., Volohonsky G., Komlosh A., Bluvshtein E., Tubi C., Steinberg P., 2003 – Biofactors. 17(1-4):139-49. pubmed

3. A spectrophotometric assay of gamma-glutamylcysteine synthetase and glutathione synthetase in crude extracts from tissues and cultured mammalian cells. Volohonsky G., Tuby C.N., Porat N., Wellman-Rousseau M., Visvikis A., Leroy P., Rashi S., Steinberg P., Stark A.A., 2002 – Chem Biol Interact. 140:49-65. pubmed

2. Gamma-glutamyl transpeptidase and glutathione biosynthesis in nontumorigenic and tumorigenic rat liver oval cell lines. Komlosh A., Volohonsky G., Porat N., Tuby C., Bluvshtein E., Steinberg P., Oesch F., Stark A.A., 2001 – Carcinogenesis 22:2009-16. pubmed

1. Inhibition of the hydrolytic and transpeptidase activities of rat kidney ?-glutamyl transpeptidase by specific monoclonal antibodies. Bluvshtein E., Glass G.A., Volohonsky G., Yaakubowitz M., Harness E., Smorodinsky N.I., Seidel A., Frank H., Steinberg P., and Stark A.A., 1999 – Eur. J. Biochem. 260: 1-12. pubmed