John J. M. Bergeron | |
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Born | Belleville, Ontario, Canada | December 22, 1946
Alma mater | McGill University Oxford University |
Known for | Calnexin Golgi apparatus Endosomal Signalling Proteomics |
Awards | Knight of National Order of Quebec (2018) McGill University Medal for Exceptional Academic Achievement (2016) Queen Elizabeth II Diamond Jubilee Medal (2012) McLaughlin Medal, Royal Society of Canada (2004) Rhodes Scholar, Oxford University (1966-69) Order of Canada (Member, 2022). |
Scientific career | |
Fields | Biochemistry, Cell Biology |
Institutions | McGill University |
John J. M. Bergeron, CM CQ FRSC [1] (born December 22, 1946) is a Canadian cell biologist and biochemist. He is an Emeritus Robert Reford Professor of Anatomy and Professor of Medicine at McGill University in Montreal, Quebec, Canada. He is a Rhodes Scholar (Class of 1966). He is best known for the discovery of calnexin, endosomal signalling and organellar proteomics.
Bergeron was born in Belleville, Ontario and grew up in and around the Montreal area, QC. He received the Montreal Science Fair award at Université de Montréal in 1961 which allowed him to pursue his studies and receive a B.Sc. in honours biochemistry McGill University in 1966. He continued his graduate work as a Rhodes Scholar at Oxford University, graduating with a D.Phil in biochemistry in 1969. From 1969 to 1971, he continued his post-doctoral training at the Rockefeller University (Supervisor: Dr. G. Palade). He then became an MRC Scientist the National Institute for Medical Research at Mill Hill, London, UK. In 1974, he opened his research lab in the Department of Anatomy and Cell Biology, McGill University. He rose through the ranks becoming full Professor in 1982 and Departmental Chair in 1996. In 2010, he was made Professor of Medicine and transferred his lab over to the MUHC-Research Institute and stayed there until his retirement in 2015.
Dr. Bergeron's major contributions are in Discovery Research. He discovered with Dr. Barry I. Posner the paradigm of endosomal signalling. [2] This paradigm defines exactly where and how hormones such as insulin and growth factors known to cause cancer act during health and disease.
Dr. Bergeron also discovered calnexin [3] with Dr. David Y. Thomas and uncovered the calnexin code along with Dr. Ari Helenius and Dr. Armando Parodi. [4] This is the first elucidation of the mechanism of protein folding through a sugar-based code. Bergeron, Thomas, Helenius and Parodi demonstrated that when these proteins are synthesized in cells, the sugars that become attached to the proteins define a code to enable calnexin to guide protein folding. [5] Correct folding is essential to form a functional protein and if newly synthesized proteins are misfolded then disease results. Calnexin through additional proteins that together makeup the calnexin cycle will not only guide folding but will also sense if folding is incorrect. When this happens, calnexin will send the incorrectly folded protein to be degraded through other sugar recognizing proteins that were again discovered with Thomas and separately by Helenius and Parodi. This represents the first protein folding code to be mechanistically solved and represents the basis for several protein misfolding diseases. [6]
Using the new technology of proteomics that Dr. Bergeron pioneered in Quebec and Canada, he elucidated the major resident proteins of the secretory pathway common to all cells. This led to the discovery of several proteins characterized for the first time involved in organ biogenesis and disease. [7]
With Dr. Michel Desjardins, Dr. Bergeron also discovered through proteomics and cell biology the importance of the transfer of endoplasmic reticulum constituents to phagosomes in antigen cross presentation in phagocytes and dendritic cells. [8]
Bergeron is also Founder of Caprion Proteomics Inc. and occupied positions of chief scientific officer, scientific advisor and chair of its scientific advisory board from 2000 to 2007. Bergeron is also past-president of the Human Proteome Organization (2004-2006) and is past-chair of its HUPO Initiatives project (2007-2008).
Bergeron has published over 240 scientific manuscripts and was continuously funded through grants from CIHR, CFI, NIH, GQ, FRQS, NCI, PENCE and MRC throughout his career. Bergeron supervised 32 graduate students, 25 post-docs and 5 visiting scientists. He has given lectures regarding his work both nationally and internationally, is a member of several societies (7), and has participated in multiple grant committees (45) and editorial boards (8) throughout his career.
Bergeron is also known as a strong advocate for Health Research in Canada through several OPEDs and interviews in several newspapers including Maclean's magazine, the National Post, the Globe and Mail, the Toronto Star, the Ottawa Citizen, the Edmonton Journal, the Montreal Gazette and The Conversation. He has given interviews regarding Canadian Science policy in the media on RDI Économie, ICI Radio-Canada and iPolitics Live. He provided an explanation of the inner workings of the cell on the Radio-Canada TV program Découverte.
Calreticulin also known as calregulin, CRP55, CaBP3, calsequestrin-like protein, and endoplasmic reticulum resident protein 60 (ERp60) is a protein that in humans is encoded by the CALR gene.
Glycomics is the comprehensive study of glycomes, including genetic, physiologic, pathologic, and other aspects. Glycomics "is the systematic study of all glycan structures of a given cell type or organism" and is a subset of glycobiology. The term glycomics is derived from the chemical prefix for sweetness or a sugar, "glyco-", and was formed to follow the omics naming convention established by genomics and proteomics.
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis.
Calnexin (CNX) is a 67kDa integral protein of the endoplasmic reticulum (ER). It consists of a large N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short, acidic cytoplasmic tail. In humans, calnexin is encoded by the gene CANX.
The terms glycans and polysaccharides are defined by IUPAC as synonyms meaning "compounds consisting of a large number of monosaccharides linked glycosidically". However, in practice the term glycan may also be used to refer to the carbohydrate portion of a glycoconjugate, such as a glycoprotein, glycolipid, or a proteoglycan, even if the carbohydrate is only an oligosaccharide. Glycans usually consist solely of O-glycosidic linkages of monosaccharides. For example, cellulose is a glycan composed of β-1,4-linked D-glucose, and chitin is a glycan composed of β-1,4-linked N-acetyl-D-glucosamine. Glycans can be homo- or heteropolymers of monosaccharide residues, and can be linear or branched.
Rudolf Aebersold is a Swiss biologist, regarded as a pioneer in the fields of proteomics and systems biology. He has primarily researched techniques for measuring proteins in complex samples, in many cases via mass spectrometry. Ruedi Aebersold is a professor of Systems biology at the Institute of Molecular Systems Biology (IMSB) in ETH Zurich. He was one of the founders of the Institute for Systems Biology in Seattle, Washington, United States where he previously had a research group.
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The unfolded protein response (UPR) is a cellular stress response related to the endoplasmic reticulum (ER) stress. It has been found to be conserved between mammalian species, as well as yeast and worm organisms.
Protein disulfide-isomerase A3 (PDIA3), also known as glucose-regulated protein, 58-kD (GRP58), is an isomerase enzyme encoded by the autosomal gene PDIA3 in humans. This protein localizes to the endoplasmic reticulum (ER) and interacts with lectin chaperones calreticulin and calnexin (CNX) to modulate folding of newly synthesized glycoproteins. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.
Glucosidase 2 subunit beta is an enzyme that in humans is encoded by the PRKCSH gene.
Secretory carrier-associated membrane protein 1 is a protein that in humans is encoded by the SCAMP1 gene.
SH3 domain-binding glutamic acid-rich-like protein is a protein that in humans is encoded by the SH3BGRL gene.
UGGT, or UDP-glucose:glycoprotein glucosyltransferase, is a soluble enzyme resident in the lumen of the endoplasmic reticulum (ER).
In molecular biology, the calreticulin protein family is a family of calcium-binding proteins. This family includes calreticulin, calnexin and camlegin.
The Human Proteome Project (HPP) is a collaborative effort coordinated by the Human Proteome Organization. Its stated goal is to experimentally observe all of the proteins produced by the sequences translated from the human genome.
Phospholipase D3, also known as PLD3, is a protein that in humans is encoded by the PLD3 gene. PLD3 belongs to the phospholipase D superfamily because it contains the two HKD motifs common to members of the phospholipase D family, however, it has no known catalytic function similar to PLD1 or PLD2. PLD3 serves as a ssDNA 5' exonuclease in antigen presenting cells. PLD3 is highly expressed in the brain in both humans and mice, and is mainly localized in the endoplasmic reticulum (ER) and the lysosome.
Kai Simons is a Finnish professor of biochemistry and cell biology and physician, living and working in Germany. He introduced the concept of lipid rafts, and coined the term trans-Golgi network. He is the co-founder and co-organizer of the European Molecular Biology Laboratory and European Molecular Biology Organization, and initiated the foundation of Max Planck Institute of Molecular Cell Biology and Genetics.
Ying Ge is a Chinese-American chemist who is a Professor of Cell and Regenerative Biology at the University of Wisconsin–Madison. Her research considers the molecular mechanisms that underpin cardiac disease. She has previously served on the board of directors of the American Society for Mass Spectrometry. In 2020 Ge was named on the Analytical Scientist Power List.
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