Delivery of newly synthesized proteins to the plasma membrane and the extracellular medium takes place in the membrane organelle of the secretory pathway. The molecular machinery behind the functional organization of this pathway is tightly controlled and is regulated by signaling. In this context, we study the role of ERK7 in Drosophila S2 cells. In addition to this classical secretion, a number of transmembrane proteins are unconventionally deposited to the plasma membrane, a pathway whose biogenesis is triggered by mechanical stress at specific stages of development. We study this unconventional secretion pathway in Drosophila as well as mammalian cells using genetics and microscopy.
About the research
Selected recent key publications
Zacharogianni, M., V. Kondylis, Y. Tang, D. Xanthakis, H. Farhan, F. Fuchs, M. Boutros and C. Rabouille (2011). ERK7 is a negative regulator of protein secretion in response to amino acid starvation by modulating Sec16 membrane association. EMBO J. 30:3684-700.
Weil, T.T., R.M. Parton, B. Herpers, J. Soetaert, T. Veenendaal, D. Xanthakis, I.M. Dobbie, J. Halstead, R. Hayashi, C. Rabouille* and I. Davis1* (2012). Drosophila patterning is established by differential association of mRNAs with P bodies. Nat. Cell Biol. 14:1305-13
Giuliani, G., F. Giuliani, T. Volk and C. Rabouille (2013).The Drosophila RNA-binding protein HOW controls the stability of dgrasp mRNA in the follicular epithelium.
Nucleic Acids Res. 42(3):1970-86.
Bellouze M, M.K. Schäfer, D. Buttigieg, G. Baillat, C. Rabouille and G. Haase (2014). Golgi fragmentation in pmn mice is due to a defective ARF1/TBCE cross talk that coordinates COPI vesicle formation and tubulin polymerization. Hum. Mol. Genet. Jun 20. pii: ddu320
Zacharogianni, M., A. Aguilera, J. Smout, T. Veenendaal, and C. Rabouille (2014). A reversible non-membrane bound stress assembly that confers cell viability by preserving COPII components during amino-acid starvation. In revision at Elife