Postdoc or PhD position: Membrane fusion - roles of membrane tethering proteins in the formation of fusion pores - University of Lausanne - job portal | jobs.myScience

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Postdoc or PhD position: Membrane fusion - roles of membrane tethering proteins in the formation of fusion pores
University of Lausanne
Published	9 December 2017
Workplace	Epalinges (Lausanne), Lake Geneva region, Switzerland
Category	Life Sciences
Position	Junior Researcher / PhD Position
Postdoc or PhD position: Membrane fusion - roles of membrane tethering proteins in the formation of fusion pores
Description Membrane fusion is fundamental to the organisation of cells. It mediates the biogenesis of organelles, vesicular traffic between them, and exo- and endocytosis. SNAREs are considered as the core engine that is sufficient to provide efficient fusion. They mechanically distort membranes and push them through a hemifusion intermediate towards the formation of a fusion pore. Our recent findings indicate, however, that tether and SM protein complexes provide critical driving force for this final step. Thus, the actual SNARE-containing fusion machinery is much bigger and more complex than hitherto thought.
Requirements Our team is now seeking a highly motivated scientist to characterize this novel aspect further and explore how tether proteins control fusion pore opening. Candidates with experience and a thorough training in biochemistry, chemistry, molecular or cell biology are particularly encouraged to apply. Knowledge of yeast genetics and advanced cellular imaging techniques is advantageous but not essential.
We offer Lausanne offers a very attractive research environment, featuring a large number of highly performant and interactive research groups, state-of-the-art technical facilities, as well as a rich cultural life and great outdoor activities. The working language is English.
Contact and Address Applications should be sent by e-mail to: andreas.mayerunil.ch. They should contain a cv, a description of your previous work, a brief statement of your research interests and objectives, and contact information of two or more referees. References: D’Agostino M, Risselada HJ & Mayer A (2016) Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition. EMBO Rep 17: 1590–1608 D’Agostino M, Risselada HJ, Lürick A, Ungermann C & Mayer A (2017) A tethering complex drives the terminal stage of SNARE-dependent membrane fusion. Nature 337: 1340 Reese C, Heise F & Mayer A (2005) Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion. Nature 436: 410–414 Pieren M, Desfougères Y, Michaillat L, Schmidt A & Mayer A (2015) Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing. J. Biol. Chem. 290: 12821–12832 Pieren M, Schmidt A & Mayer A (2010) The SM protein Vps33 and the t-SNARE H(abc) domain promote fusion pore opening. Nat Struct Mol Biol 17: 710–717 Strasser B, Iwaszkiewicz J, Michielin O & Mayer A (2011) The V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles. EMBO J 30: 4126–4141 Gopaldass N, Fauvet B, Lashuel H, Roux A & Mayer A (2017) Membrane scission driven by the PROPPIN Atg18. EMBO J : e201796859
Email
Phone 0041 (0)21 692 5704
Web www.unil.ch
Warning: this advert is not valid anymore. (2018-01-18)
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