John J. M. Bergeron

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John J. M. Bergeron
Born (1946-12-22) December 22, 1946 (age 76)
Nationality Canadian
Alma mater McGill University
Oxford University
Known for Calnexin
Golgi apparatus
Endosomal Signalling
Proteomics
AwardsKnight 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.

Contents

Education

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.

Research and scientific career

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).

Publications and scholarly activities

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.

Awards and recognition

Related Research Articles

<span class="mw-page-title-main">Calreticulin</span> Soluble protein

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.

<span class="mw-page-title-main">Chaperone (protein)</span> Proteins assisting in protein folding

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.

<span class="mw-page-title-main">Calnexin</span> Mammalian protein found in Homo sapiens

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.

<span class="mw-page-title-main">Ruedi Aebersold</span> Swiss biologist (born 1954)

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, where he previously had a research group.

<span class="mw-page-title-main">Uteroglobin</span> Protein-coding gene in the species Homo sapiens

Uteroglobin, or blastokinin, also known as secretoglobin family 1A member 1 (SCGB1A1), is a protein that in humans is encoded by the SCGB1A1 gene.

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.

<span class="mw-page-title-main">PDIA3</span> Protein-coding gene in the species Homo sapiens

Protein disulfide-isomerase A3 (PDIA3), also known as glucose-regulated protein, 58-kD (GRP58), is an isomerase enzyme. 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.

The epididymal secretory protein E1, also known as NPC2( Niemann-Pick intracellular cholesterol transporter 2), is one of two main lysosomal transport proteins that assist in the regulation of cellular cholesterol by exportation of LDL-derived cholesterol from lysosomes. Lysosomes have digestive enzymes that allow it to break down LDL particles to LDL-derived cholesterol once the LDL particle is engulfed into the cell via receptor mediated endocytosis.

<span class="mw-page-title-main">SCAMP1</span> Protein-coding gene in the species Homo sapiens

Secretory carrier-associated membrane protein 1 is a protein that in humans is encoded by the SCAMP1 gene.

<span class="mw-page-title-main">DNAJC5</span> Protein-coding gene in the species Homo sapiens

DnaJ homolog subfamily C member 5, also known as cysteine string protein or CSP is a protein, that in humans encoded by the DNAJC5 gene. It was first described in 1990.

<span class="mw-page-title-main">SH3BGRL</span> Protein-coding gene in the species Homo sapiens

SH3 domain-binding glutamic acid-rich-like protein is a protein that in humans is encoded by the SH3BGRL gene.

<span class="mw-page-title-main">UGGT</span> Class of enzymes

UGGT, or UDP-glucose:glycoprotein glucosyltransferase, is a soluble enzyme resident in the lumen of the endoplasmic reticulum (ER).

<span class="mw-page-title-main">Calreticulin protein family</span>

In molecular biology, the calreticulin protein family is a family of calcium-binding proteins. This family includes Calreticulin, Calnexin and Camlegin.

Secretomics is a type of proteomics which involves the analysis of the secretome—all the secreted proteins of a cell, tissue or organism. Secreted proteins are involved in a variety of physiological processes, including cell signaling and matrix remodeling, but are also integral to invasion and metastasis of malignant cells. Secretomics has thus been especially important in the discovery of biomarkers for cancer and understanding molecular basis of pathogenesis. The analysis of the insoluble fraction of the secretome has been termed matrisomics.

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<span class="mw-page-title-main">Kai Simons</span>

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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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References

  1. 1 2 "Order of Canada appointees – December 2022". The Governor General of Canada. 29 December 2022. Retrieved 29 December 2022.
  2. Bergeron, J.J.M.; Di Guglielmo, G.M.; Dahan, S.; Dominguez, M.; Posner, B.I. (2016). "Spatial and Temporal Regulation of Receptor Tyrosine Kinase Activation and Intracellular Signal Transduction". Annu Rev Biochem. 85: 573–597. doi: 10.1146/annurev-biochem-060815-014659 . PMID   27023845.
  3. Ou, W.J.; Cameron, P.H.; Thomas, D.Y.; Bergeron, J.J.M. (1993). "Association of folding intermediates of glycoproteins with calnexin during protein maturation". Nature. 364: 771–776. doi:10.1038/364771a0. PMID   8102790.
  4. Schrag, J.D.; Procopio, D.O.; Cygler, M.; Thomas, D.Y.; Bergeron, J.J.M. (2003). "Lectin control of protein folding and sorting in the secretory pathway". Trends Biochem Sci. 28: 49–57. doi:10.1016/S0968-0004(02)00004-X. PMID   12517452.
  5. Zapun, A.; Petrescu, S.M.; Rudd, P.M.; Dwek, R.A.; Thomas, D.Y.; Bergeron, J.J.M. (1997). "Conformation-independent binding of monoglucosylated ribonuclease B to calnexin". Cell. 88: 29–38. doi: 10.1016/S0092-8674(00)81855-3 . PMID   9019402.
  6. Dickson, K.M.; Bergeron, J.J.M.; Shames, I.; Colby, J.; Nguyen, D.T.; Chevert, E.; Thomas, D.T.; Snipes, G.J. (2002). "Association of calnexin with mutant peripheral myelin protein-22 ex vivo: a basis for "gain-of-function" ER diseases". Proc Natl Acad Sci U S A. 99: 9852–9857. doi:10.1073/pnas.152621799. PMC   125041 . PMID   12119418.
  7. Gilchrist, A.; Au, C.E.; Hiding, J.; Bell, A.W.; Fernandez-Rodriguez, J.; Lesimple, S.; Nagaya, H.; Roy, L.; Gosline, S.J.; Hallett, M.; Paiement, J.; Kearney, R.E.; Nilsson, T.; Bergeron, J.J.M. (2006). "Quantitative proteomics analysis of the secretory pathway". Cell. 127: 1265–1281. doi: 10.1016/j.cell.2006.10.036 . PMID   17174899.
  8. Gagnon, E.; Duclos, S.; Rondeau, C.; Chevet, E.; Cameron, P.H.; Steele-Mortimer, O.; Paiement, J.; Bergeron, J.J.M.; Desjardins, M. (2002). "Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages". Cell. 110: 119–131. doi: 10.1016/S0092-8674(02)00797-3 . PMID   12151002.