Gaia Pigino is a biologist, currently Associate Head of the Structural Biology Center at Human Technopole, after 9 years as Research Group Leader at the Max Planck Institute CBG in Dresden. She collaborate with Alessandro Vannini to develop the Centre for Structural Biology. Gaia’s laboratory studies molecular mechanisms and principles of self-organisation in cilia and other subcellular structures that are of fundamental importance for human health and disease.
Since 2021 Associate Head of the Structural Biology Center at Human Technopole, Milan, Italy
Since 2012 Research Group Leader at MPI-CBG, the Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
2010-2012 Postdoctoral EMBO Long Term fellow Laboratory of Biomolecular Research (BMR), Department of Biology and Chemistry, Paul Scherer Institute (PSI) Switzerland. Supervisor: Prof. T. Ishikawa.
2009-2011 Postdoctoral researcher Institute for Molecular Biology and Biophysics, Swiss Federal Institute of Technology (ETH Zürich), Zurich, Switzerland. Supervisor: Prof. T. Ishikawa.
2007-2009 Postdoctoral MIUR research fellow Fellowship of the “Ministero Italiano dell’Istruzione, dell’Università e della Ricerca”. Laboratory of Cryotechniques for Electron Microscopy, Department of Evolutionary Biology, University of Siena. Supervisor: Prof. P. Lupetti.
2009 Participant at the Physiology Course at MBL in Woods Hole Marine Biological Laboratory, Woods Hole. Directors: Dyche Mullins and Claire Waterman.
2003-2007 Ph.D. Student (Ph.D. Fellowship by the Italian government “Ministero Italiano dell’Istruzione, dell’Università e della Ricerca”). Department of Evolutionary Biology, University of Siena. Supervisor: Prof. F. Bernini and Prof. C. Leonzio.
2002 Diploma in Natural Science (Summa cum laude). University of Siena, Italy. Thesis supervisors: Prof. C. Leonzio and Prof. F. Bernini.
2003 Research Associate. Department of Environmental Sciences G. Sarfatti, University of Siena. Advisor: Prof. C. Leonzio
AWARDS and FUNDING
2019 DFG Grant – GAČR-DFG Cooperation
2018 PoL starting fellowship (from the Dresden Excellence Cluster ‘Physics of Life’)
2018 Keith R. Porter Fellow Award for Cell Biology
2018 ERC Consolidator Grant (ERC-2018-COG N#819826 CiliaTubulinCode)
2018 Excellence Cluster ‘Physics of Life’, as a core Principal Investigator
2010 EMBO Long Term fellowship
2009 Scholarship from the Marine Biological Laboratory (Woods Hole, Massachusetts) MBL Physiology Course.
2007 Post-Doctoral Research fellowship from the “Ministero Italiano dell’Istruzione, dell’Università e della Ricerca (MIUR)”.
2003 Ph.D. Fellowship from the “Ministero Italiano dell’Istruzione, dell’Università e della Ricerca (MIUR)”.
Fellowship to students and postdocs
2019 HFSP Postdoc fellowship to Adrian Nievergelt
2018 EMBO Long Term Fellowship to Adrian Nievergelt
2017 Marie Curie Fellowship to Adam Schröfel (H2020-MSCA-IF-2016)
2015 DIGS-BB Fellowship to Guendalina Marini
2012 DIGS-BB Fellowship to Ludek Stepanek
TEACHING AND OUTREACH
Since 2013 she is invited Lecturer for Master and PhD courses of the Technical University Dresden, the MPI-CBG and the CSBD in Dresden. Since 2012 she served in about 15 Thesis Advisory Committees (TAC) PhD students at the MPI-CBG, Dresden, Germany, the Universitätsklinikum Hamburg-Eppendorf, Hamburg, Germany, and the EPFL Lausanne, Switzerland.
IN the last four years (since 2016) she participated to more than 40 events between international scientific conferences, workshops and invited seminars in the roles of invited speaker, conference chair person, or organizer.
Reviewer for Journals and Granting Agencies:
Journals: Nature; Science; Nature Methods; Nature Structural and Molecular Biology; Journal of Cell Biology; eLife; Proceedings of the National Academy of Sciences (PNAS); Journal of Structural Biology; Molecular Biology of the Cell; Scientific Reports; Nature Communications; Tissue and Cell; and others.
Agencies: European Research Council (ERC) Brussels (remote evaluator); Deutsche Forschungsgemeinschaft (DFG) Germany; Agence National de la Recherche (ANR), France.
01/2021 - Science
Posttranslational modifications of the microtubule cytoskeleton have emerged as key regulators of cellular functions, and their perturbations have been linked to a growing number of human pathologies. Tubulin glycylation modifies microtubules specifically in cilia and flagella, but its functional and mechanistic roles remain unclear. In this study, we generated a mouse model entirely lacking tubulin […]
09/2020 - Nature Structural Molecular Biology
Primary cilia are microtubule-based organelles that are important for signaling and sensing in eukaryotic cells. Unlike the thoroughly studied motile cilia, the three-dimensional architecture and molecular composition of primary cilia are largely unexplored. Yet, studying these aspects is necessary to understand how primary cilia function in health and disease. We developed an enabling method for […]
05/2016 - Science
The cilium is a large macromolecular machine that is vital for motility, signaling, and sensing in most eukaryotic cells. Its conserved core structure, the axoneme, contains nine microtubule doublets, each comprising a full A-microtubule and an incomplete B-microtubule. However, thus far, the function of this doublet geometry has not been understood. We developed a time-resolved […]
05/2012 - Journal of Structural Biology
Comparative structural analysis of eukaryotic flagella and cilia from Chlamydomonas, Tetrahymena, and sea urchins
Although eukaryotic flagella and cilia all share the basic 9 + 2 microtubule-organization of their internal axonemes, and are capable of generating bending-motion, the waveforms, amplitudes, and velocities of the bending-motions are quite diverse. To explore the structural basis of this functional diversity of flagella and cilia, we here compare the axonemal structure of three different organisms with […]
11/2011 - Journal of Cell Biology
Radial spokes (RSs) are ubiquitous components in the 9 + 2 axoneme thought to be mechanochemical transducers involved in local control of dynein-driven microtubule sliding. They are composed of >23 polypeptides, whose interactions and placement must be deciphered to understand RS function. In this paper, we show the detailed three-dimensional (3D) structure of RS in […]