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
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09/2005 - Cell
Rab Conversion as a Mechanism of Progression from Early to Late Endosomes
The mechanisms of endosome biogenesis and maintenance are largely unknown. The small GTPases Rab5 and Rab7 are key determinants of early and late endosomes, organizing effector proteins into specific membrane subdomains. Whether such Rab machineries are indefinitely maintained on membranes or can disassemble in the course of cargo transport is an open question. Here, we […]
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08/1999 - Cell
Oligomeric Complexes Link Rab5 Effectors with NSF and Drive Membrane Fusion via Interactions between EEA1 and Syntaxin 13
SNAREs and Rab GTPases cooperate in vesicle transport through a mechanism yet poorly understood. We now demonstrate that the Rab5 effectors EEA1 and Rabaptin-5/Rabex-5 exist on the membrane in high molecular weight oligomers, which also contain NSF. Oligomeric assembly is modulated by the ATPase activity of NSF. Syntaxin 13, the t-SNARE required for endosome fusion, […]
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02/1999 - Nature
The Rab5 effector EEA1 is a core component of endosome docking
Intracellular membrane docking and fusion requires the interplay between soluble factors and SNAREs. The SNARE hypothesis1 postulates that pairing between a vesicular v-SNARE and a target membrane z-SNARE is the primary molecular interaction underlying the specificity of vesicle targeting as well as lipid bilayer fusion. This proposal is supported by recent studies using a minimal artificial […]
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09/1992 - Cell
The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
We have investigated the in vivo functional role of rab5, a small GTPase associated with the plasma membrane and early endosomes. Wild-type rab5 or rab5ile 133, a mutant protein defective in GTP binding, was overexpressed in baby hamster kidney cells. In cells expressing the rab5ile 133 protein, the rate of endocytosis was decreased by 50% […]
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07/1990 - Cell
Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments
A set of 11 clones encoding putative GTP binding proteins highly homologous to the yeast YPT1SEC4 gene products have been isolated from an MDCK cell cDNA library. We localized three of the corresponding proteins in mammalian cells by using affinity-purified antibodies in immunofluorescence and immunoelectron microscopy studies. One, the MDCK homolog of rab2, is associated […]
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