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The Gatsogiannis Lab is dedicated to elucidate the architecture of complex nanomachines, by their direct visualisation using cryoEM and image processing, at resolutions ranging from nanometer to near atomic level of detail. This technique allows us to study their macromolecular structure at near native conditions and in combination with biochemical and biophysical assays, can provide crucial mechanistic insight and thus, a solid framework to understand their mode of action.
Pore-forming proteins represent a unique class of highly specific lipid-binding proteins, which undergo a sophisticated metamorphosis from a soluble prepore, to a transmembrane pore state. We are especially interested to understand the underlying mechanisms of those pore-forming proteins that are capable to insert into membranes, in a regulated manner.
Peroxisomal protein import pore
The import of natively folded proteins into the peroxisomal matrix is directed by specific targeting signals. Cargo-proteins are imported via binding to a cytosolic receptor, which undergoes a conformation change and becomes an integral component of a transient import pore. So far structures of the import pores, needed to understand the translocation mechanism, are missing. Our lab is dedicated to elucidate the 3D- structure of the peroxisomal translocation pores, facilitating the PTS1- and PTS2-dependent protein import into the organellar matrix.
The development of novel reagents, including nanodiscs and amphipols, has greatly facilitated functional and structural studies of integral membrane proteins (IMPs). We we are interested in developing novel and delicate methodologies, to optimize the sample quality of IMPs for high-resolution structural analysis by cryoEM.
Pascal Lill (phd student, joins Jan. 2017)
- Diploma in Biology, JGU Mainz, Germany (2005)
- Dr. rer. nat, JGU Mainz, Germany, (2009)
- Postdoc, JGU Mainz, Germany, (2010) (with J. Markl)
- Postdoc, Max Planck Institute for Molecular Physiology, Dortmund, Germany (2010-2015) (with S. Raunser)
- Project Group Leader, Department of Structural Biochemistry, Max Planck Institute for Molecular Physiology, Dortmund, Germany (since 2016)
- Project Group Leader, Research Unit 1905, “Structure and Function of the Peroxisomal Translocon (PerTrans)” (since 2016)
Gatsogiannis C, Merino F, Serdiuk T, Prumbaum D, Roderer D, Leidreiter F, Meusch D, Müller DJ, and Raunser S (2016). Membrane insertion of a Tc toxin in atomic detail. Nature Structural and Molecular Biology 23(10):884-890.
Gatsogiannis C, Hofnagel O, Markl J, Raunser S (2015). Structure of Mega-Hemocyanin reveals protein origami in snails. Structure 23(1):93-103.
Meusch D, Gatsogiannis C, Efremov R, Lang A, Hofnagel O, Vetter I, Aktories K, Raunser S (2014). Mechanism of Tc toxin action revealed in molecular detail. Nature 508(7494):61-5.
Gatsogiannis C, Lang A, Meusch D, Pfaumann V, Hofnagel O, Benz R, Aktories K, Raunser S (2013). A syringe-like injection mechanism in Photorhabdus luminescens toxins. Nature. 495(7442):520-23
Bröcker C, Kuhlee A, Gatsogiannis C, Balderhaar HJ, Hönscher C, Engelbrecht-Vandré S, Ungermann C, Raunser S (2013). Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex. Proc Natl Acad Sci U S A . 109(6):1991-6