Gaia Pigino | |
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Nationality | Italian |
Alma mater | University of Siena (Diploma, PhD) |
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Website | Pigino Lab |
Gaia Pigino is the Associate Head of the Structural Biology Research Center [1] and Research Group Leader of the Pigino Group [2] at the Human Technopole in Milan, Italy. [3]
Pigino studied Natural Science at the University of Siena in Italy, finishing with a Diploma in 2002. From 2003 to 2007, she earned her Ph.D., working in the Department of Evolutionary Biology at the University of Siena, supervised by Prof Fabio Bernini and Prof Claudio Leonzio. [4]
From 2007 to 2009, Pigino was employed at the Laboratory of Cryotechniques for Electron Microscopy in the Department of Evolutionary Biology of the University of Siena, under the guidance of Prof. Pietro Lupetti. she continued her postgraduate studies, also attending the prestigious Physiology course at the Marine Biological Laboratory (MBL) in Woods Hole (Massachusetts, USA). Subsequently, Gaia Pigino worked with Prof. Takashi Ishikawa at the ETH Zurich from 2009 to 2011 and then at the Paul Scherrer Institute from 2011 to 2012. [5] [6] [7] [8]
From 2012 to 2021, Gaia Pigino was a Research Group Leader at the Max Planck Institute of Molecular Cell Biology and Genetics in Dresden, Germany. [9] [10] [11]
Since 2021, Gaia Pigino has been the Associate Head of the Structural Biology Research Center and Research Group Leader of the Pigino Group at the Human Technopole in Milan, Italy. [12] [13] [14]
Her research group operates at the intersection of structural and molecular cell biology, utilizing the most current methodologies from both areas to investigate the structure and dynamics of molecular machines that participate in the assembly and function of motile and primary cilia. Their overarching objective is to comprehend the fundamental molecular mechanisms of ciliary functions, as well as their malfunctions in ciliopathies.
Gaia Pigino is an internationally well-known biologist. Hence, she is frequently invited to workshops, [15] [16] seminars [17] and conferences [18] [19] [20] [21] in the field.
Structural biology, as defined by the Journal of Structural Biology, deals with structural analysis of living material at every level of organization.
The cilium is a membrane-bound organelle found on most types of eukaryotic cell. Cilia are absent in bacteria and archaea. The cilium has the shape of a slender threadlike projection that extends from the surface of the much larger cell body. Eukaryotic flagella found on sperm cells and many protozoans have a similar structure to motile cilia that enables swimming through liquids; they are longer than cilia and have a different undulating motion.
The evolution of flagella is of great interest to biologists because the three known varieties of flagella – each represent a sophisticated cellular structure that requires the interaction of many different systems.
Inositol trisphosphate receptor (InsP3R) is a membrane glycoprotein complex acting as a Ca2+ channel activated by inositol trisphosphate (InsP3). InsP3R is very diverse among organisms, and is necessary for the control of cellular and physiological processes including cell division, cell proliferation, apoptosis, fertilization, development, behavior, learning and memory. Inositol triphosphate receptor represents a dominant second messenger leading to the release of Ca2+ from intracellular store sites. There is strong evidence suggesting that the InsP3R plays an important role in the conversion of external stimuli to intracellular Ca2+ signals characterized by complex patterns relative to both space and time, such as Ca2+ waves and oscillations.
In molecular biology, an axoneme, also called an axial filament, is the microtubule-based cytoskeletal structure that forms the core of a cilium or flagellum. Cilia and flagella are found on many cells, organisms, and microorganisms, to provide motility. The axoneme serves as the "skeleton" of these organelles, both giving support to the structure and, in some cases, the ability to bend. Though distinctions of function and length may be made between cilia and flagella, the internal structure of the axoneme is common to both.
The Max Planck Institute of Biochemistry is a research institute of the Max Planck Society located in Martinsried, a suburb of Munich. The institute was founded in 1973 by the merger of three formerly independent institutes: the Max Planck Institute of Biochemistry, the Max Planck Institute of Protein and Leather Research, and the Max Planck Institute of Cell Chemistry.
Cryogenic electron tomography (cryoET) is an imaging technique used to reconstruct high-resolution (~1–4 nm) three-dimensional volumes of samples, often biological macromolecules and cells. cryoET is a specialized application of transmission electron cryomicroscopy (CryoTEM) in which samples are imaged as they are tilted, resulting in a series of 2D images that can be combined to produce a 3D reconstruction, similar to a CT scan of the human body. In contrast to other electron tomography techniques, samples are imaged under cryogenic conditions. For cellular material, the structure is immobilized in non-crystalline, vitreous ice, allowing them to be imaged without dehydration or chemical fixation, which would otherwise disrupt or distort biological structures.
MRC is a file format that has become an industry standard in cryo-electron microscopy (cryoEM) and electron tomography (ET), where the result of the technique is a three-dimensional grid of voxels each with a value corresponding to electron density or electric potential. It was developed by the MRC Laboratory of Molecular Biology. In 2014, the format was standardised. The format specification is available on the CCP-EM website.
Eva Nogales is a Spanish-American biophysicist at the Lawrence Berkeley National Laboratory and a professor at the University of California, Berkeley, where she served as head of the Division of Biochemistry, Biophysics and Structural Biology of the Department of Molecular and Cell Biology (2015–2020). She is a Howard Hughes Medical Institute investigator.
The prokaryotic cytoskeleton is the collective name for all structural filaments in prokaryotes. It was once thought that prokaryotic cells did not possess cytoskeletons, but advances in visualization technology and structure determination led to the discovery of filaments in these cells in the early 1990s. Not only have analogues for all major cytoskeletal proteins in eukaryotes been found in prokaryotes, cytoskeletal proteins with no known eukaryotic homologues have also been discovered. Cytoskeletal elements play essential roles in cell division, protection, shape determination, and polarity determination in various prokaryotes.
Ciliogenesis is defined as the building of the cell's antenna or extracellular fluid mediation mechanism. It includes the assembly and disassembly of the cilia during the cell cycle. Cilia are important appendages of cells and are involved in numerous activities such as cell signaling, processing developmental signals, and directing the flow of fluids such as mucus over and around cells. Due to the importance of these cell processes, defects in ciliogenesis can lead to numerous human diseases related to non-functioning cilia known as ciliopathies.
Ueli Aebi is a Swiss structural biologist and co-founder of the Maurice E. Müller Institute for Structural Biology at the Biozentrum University of Basel.
Jacques Dubochet is a retired Swiss biophysicist. He is a former researcher at the European Molecular Biology Laboratory in Heidelberg, Germany, and an honorary professor of biophysics at the University of Lausanne in Switzerland.
Cryogenic electron microscopy (cryo-EM) is a cryomicroscopy technique applied on samples cooled to cryogenic temperatures. For biological specimens, the structure is preserved by embedding in an environment of vitreous ice. An aqueous sample solution is applied to a grid-mesh and plunge-frozen in liquid ethane or a mixture of liquid ethane and propane. While development of the technique began in the 1970s, recent advances in detector technology and software algorithms have allowed for the determination of biomolecular structures at near-atomic resolution. This has attracted wide attention to the approach as an alternative to X-ray crystallography or NMR spectroscopy for macromolecular structure determination without the need for crystallization.
Lori Anne Passmore is a Canadian/British cryo electron microscopist and structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) at the University of Cambridge. She is known for her work on multiprotein complexes involved in gene expression and development of new supports for cryo-EM.
RVxP motif is a protein motif involved in localizing proteins into cilia.
J. Richard McIntosh is a Distinguished Professor Emeritus in Molecular, Cellular, and Developmental Biology at the University of Colorado Boulder. McIntosh first graduated from Harvard with a BA in Physics in 1961, and again with a Ph.D. in Biophysics in 1968. He began his teaching career at Harvard but has spent most of his career at the University of Colorado Boulder. At the University of Colorado Boulder, McIntosh taught biology courses at both the undergraduate and graduate levels. Additionally, he created an undergraduate course in the biology of cancer towards the last several years of his teaching career. McIntosh's research career looks at a variety of things, including different parts of mitosis, microtubules, and motor proteins.
Stefan Raunser is a German scientist and structural biologist specializing in membrane proteins, the cytoskeleton, toxins, and sarcomere structural biochemistry. Since 2014, he has been a director at the Max Planck Institute of Molecular Physiology in Dortmund, Germany.
Julia Mahamid is a cell biologist, structural biologist, and electron microscopist at the European Molecular Biology Laboratory in Heidelberg, Germany, who utilizes biomolecular condensates and advanced cellular cryo-electron tomography to enhance the comprehension of the functional organization of the cytoplasm. She leads the Mahamid Group.
Tanmay A. M. Bharat is a programme leader in the Structural Studies Division of the MRC Laboratory of Molecular Biology. He and his group use electron tomography, together with several structural and cell biology methods to study the cell surfaces of bacteria and archaea. His work has increased the understanding of how surface molecules help in the formation of multicellular communities of prokaryotes, examples of which include biofilms and microbiomes. He has been awarded several prizes and fellowships for his work.