Marino Zerial
- Director, Directorate
- Group Leader, Zerial Group
Marino Zerial graduated in biology at the University of Trieste (Italy) in 1982 with a thesis on lysosomal storage disorders. He conducted post-doctoral experiences at the Institut Jacques Monod (Paris, France) and at the European Molecular Biology Laboratory, EMBL (Heidelberg, Germany). He became group leader at the EMBL in 1989 and Max Planck Director as well as co-founder of the Max Planck Institute of Molecular Cell Biology and Genetics, MPI-CBG, (Dresden, Germany) in 1998. In addition, he is Honorary Professor at the Medical Faculty, Technische Universität Dresden (Germany).
Marino Zerial has made key contributions towards the understanding of the molecular mechanisms of endocytosis. His work on Rab GTPases as master regulators of organelle biogenesis and membrane fusion has established key principles which are textbook knowledge. He has been working on various translational projects, including the role of endocytosis in bacterial infection, development of image-based high content screenings, delivery of macromolecule therapeutics and studies of human liver diseases.
Marino Zerial was awarded several international research prizes, such as the 1994 FEBS Anniversary Prize, the Chiara D’Onofrio Prize (1999), the Gottfried Wilhelm Leibniz Prize (2006), and the Fritz Lipmann Honorary Lecture, Award of the German Society for Biochemistry and Molecular Biology (2019). He was elected EMBO Member in 1996 and Member of the Istituto Veneto di Scienze, Lettere ed Arti in 2019. Furthermore, he has recently been elected International Honorary Member of the American Academy of Arts and Sciences (2021).
Publications
-
05/2023 - Nature Physics
Two-component molecular motor driven by a GTPase cycle
ATPases are a group of enzymes that can cyclically convert the free energy of ATP hydrolysis into mechanical work. GTPases are another class of enzymes that are predominantly associated with signal transduction processes, but their role in mechanotransduction is less established. It was previously shown that the binding of the GTPase Rab5 to the tethering […]
-
12/2019
Three-dimensional spatially resolved geometrical and functional models of human liver tissue reveal new aspects of NAFLD progression
Early disease diagnosis is key to the effective treatment of diseases. Histopathological analysis of human biopsies is the gold standard to diagnose tissue alterations. However, this approach has low resolution and overlooks 3D (three-dimensional) structural changes resulting from functional alterations. Here, we applied multiphoton imaging, 3D digital reconstructions and computational simulations to generate spatially resolved […]
-
08/2016 - Nature
An endosomal tether undergoes an entropic collapse to bring vesicles together
An early step in intracellular transport is the selective recognition of a vesicle by its appropriate target membrane, a process regulated by Rab GTPases via the recruitment of tethering effectors1,2,3,4. Membrane tethering confers higher selectivity and efficiency to membrane fusion than the pairing of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) alone5,6,7. Here we address the […]
-
05/2012 - Nature
Rab5 is necessary for the biogenesis of the endolysosomal system in vivo
An outstanding question is how cells control the number and size of membrane organelles. The small GTPase Rab5 has been proposed to be a master regulator of endosome biogenesis. Here, to test this hypothesis, we developed a mathematical model of endosome dependency on Rab5 and validated it by titrating down all three Rab5 isoforms in […]
-
05/2009 - Nature
Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes
Rab GTPases and SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) are evolutionarily conserved essential components of the eukaryotic intracellular transport system. Although pairing of cognate SNAREs is sufficient to fuse membranes in vitro, a complete reconstitution of the Rab–SNARE machinery has never been achieved. Here we report the reconstitution of the early endosomal canine Rab5 GTPase, its […]
Previous page