David Ron

Last updated

David Ron
Professor David Ron FMedSci FRS.jpg
Portrait via the Royal Society (2014)
Born1955
Israel
Alma mater Technion – Israel Institute of Technology
SpouseAnne Crozat
ChildrenThomas Ron
Awards
Scientific career
Fields
Institutions
Academic advisors Joel F. Habener
Website ron.cimr.cam.ac.uk

David Ron FRS is a British biochemist.

Biography and family

Raised in an academic family - his parents, Arza and Amiram Ron, were professors of Chemistry and Physics at the Technion and his younger sister Dana Ron Goldreich is a computer scientists at Tel Aviv University - in 1972 he graduated from Municipal High-school III in נוה שאנן, חיפה

Contents

Higher education and career

Awarded a medical degree from the Faculty of Medicine, Technion in Haifa Israel in 1980, he went to medical internship and residency training at Mount Sinai Medical Center, in New York City and in 1989 completed subspecialty training in Endocrinology at Massachusetts General Hospital in Boston, followed by four-years of post-doctoral research training with Joel Habner a Howard Hughes Medical Institute Researcher at Harvard Medical School. From 1992 to 2009 he was a member of the faculty at the Skirball Institute of Biomolecular Medicine of New York University School of Medicine and in 2010 he moved to The Clinical School of Cambridge University where he serves as a Wellcome Trust Principal Research Fellow and the Professor of Cellular Pathophysiology and Clinical Biochemistry with a laboratory based at the Cambridge Institute for Medical Research.

Research

His laboratory researches molecular mechanisms by which secretory cells adapt to the burden of unfolded proteins in their endoplasmic reticulum. [3]

Awards and honours

Ron was elected a Fellow of the Royal Society (FRS) in 2014. His nomination reads:

David Ron has pioneered our understanding of how cells cope with the stress induced by protein misfolding in the endoplasmic reticulum. This stress is increasingly recognised to contribute to many diseases including endocrine disorders and neurodegeneration. Among many achievements, he has deciphered the molecular mechanism by which cells match protein synthesis rates to protein folding in the secretory pathway. His greatest conceptual contribution has been to reveal the precariousness of the protein folding environment in the ER and to highlight how it is challenged by subtle failure of homeostasis – concepts with both fundamental implications to biology and therapeutic application. [1]

Ron was elected a Fellow of the Academy of Medical Sciences (FMedSci) in 2013. His nomination reads

David Ron is Professor of Cellular Pathophysiology and Clinical Biochemistry at the University of Cambridge. Protein misfolding in the endoplasmic reticulum (ER stress) is implicated in processes from neurodegeneration to endocrine disorders. David Ron has been at the forefront of this confluence of Cell Biology and Pathophysiology. He identified the transcription factor CHOP and discovered its role in deregulating adipose tissue development in liposarcoma. He identified the ER stress transducer PERK, establishing the molecular mechanism by which unfolded protein stress regulates protein synthesis and identified the long-sought mammalian counterpart of the yeast master regulator of gene expression in the UPR, IRE1. An endocrinologist by training, he remains committed to laboratory-based disease-oriented research. [2]

Related Research Articles

<span class="mw-page-title-main">Endoplasmic reticulum</span> Cell organelle that synthesizes, folds and processes proteins

The endoplasmic reticulum (ER) is, in essence, the transportation system of the eukaryotic cell, and has many other important functions such as protein folding. It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae, and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa.

<span class="mw-page-title-main">Endomembrane system</span> Membranes in the cytoplasm of a eukaryotic cell

The endomembrane system is composed of the different membranes (endomembranes) that are suspended in the cytoplasm within a eukaryotic cell. These membranes divide the cell into functional and structural compartments, or organelles. In eukaryotes the organelles of the endomembrane system include: the nuclear membrane, the endoplasmic reticulum, the Golgi apparatus, lysosomes, vesicles, endosomes, and plasma (cell) membrane among others. The system is defined more accurately as the set of membranes that forms a single functional and developmental unit, either being connected directly, or exchanging material through vesicle transport. Importantly, the endomembrane system does not include the membranes of plastids or mitochondria, but might have evolved partially from the actions of the latter.

In cell biology, microsomes are heterogeneous vesicle-like artifacts re-formed from pieces of the endoplasmic reticulum (ER) when eukaryotic cells are broken-up in the laboratory; microsomes are not present in healthy, living cells.

<span class="mw-page-title-main">Peter Walter</span> German-American molecular biologist and biochemist

Peter Walter is a German-American molecular biologist and biochemist and is Director of the Bay Area Institute of Science at Altos Labs, Professor at the University of California, San Francisco (UCSF). He was a Howard Hughes Medical Institute (HHMI) Investigator until 2022.

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">Binding immunoglobulin protein</span> Protein-coding gene in the species Homo sapiens

Binding immunoglobulin protein (BiPS) also known as 78 kDa glucose-regulated protein (GRP-78) or heat shock 70 kDa protein 5 (HSPA5) is a protein that in humans is encoded by the HSPA5 gene.

<span class="mw-page-title-main">DNA damage-inducible transcript 3</span> Protein-coding gene in the species Homo sapiens

DNA damage-inducible transcript 3, also known as C/EBP homologous protein (CHOP), is a pro-apoptotic transcription factor that is encoded by the DDIT3 gene. It is a member of the CCAAT/enhancer-binding protein (C/EBP) family of DNA-binding transcription factors. The protein functions as a dominant-negative inhibitor by forming heterodimers with other C/EBP members, preventing their DNA binding activity. The protein is implicated in adipogenesis and erythropoiesis and has an important role in the cell's stress response.

<span class="mw-page-title-main">ERN1</span> Protein-coding gene in the species Homo sapiens

The serine/threonine-protein kinase/endoribonuclease inositol-requiring enzyme 1 α (IRE1α) is an enzyme that in humans is encoded by the ERN1 gene.

<span class="mw-page-title-main">Derlin-1</span> Protein involved in retrotranslocation of specific misfolded proteins and in ER stress

Derlin-1 also known as degradation in endoplasmic reticulum protein 1 is a membrane protein that in humans is encoded by the DERL1 gene. Derlin-1 is located in the membrane of the endoplasmic reticulum (ER) and is involved in retrotranslocation of specific misfolded proteins and in ER stress. Derlin-1 is widely expressed in thyroid, fat, bone marrow and many other tissues. The protein belongs to the Derlin-family proteins consisting of derlin-1, derlin-2 and derlin-3 that are components in the endoplasmic reticulum-associated protein degradation (ERAD) pathway. The derlins mediate degradation of misfolded lumenal proteins within ER, and are named ‘der’ for their ‘Degradation in the ER’. Derlin-1 is a mammalian homologue of the yeast DER1 protein, a protein involved in the yeast ERAD pathway. Moreover, derlin-1 is a member of the rhomboid-like clan of polytopic membrane proteins.

<span class="mw-page-title-main">Tom Rapoport</span> German-American cell biologist (born 1947)

Tom Abraham Rapoport is a German-American cell biologist who studies protein transport in cells. Currently, he is a professor at Harvard Medical School and a Howard Hughes Medical Institute investigator. Born in Cincinnati, Ohio, he grew up in East Germany. In 1995 he accepted an offer to become a professor at Harvard Medical School. In 1997 he became an investigator of the Howard Hughes Medical Institute. He is a member of the American and German National Academies of Science.

Beta cells are heavily engaged in the synthesis and secretion of insulin. They are therefore particularly sensitive to endoplasmic reticulum (ER) stress and the subsequent unfolded protein response (UPR). Severe or prolonged episodes of ER stress can lead to the death of beta cells, which can contribute to the development of both Type I and Type II diabetes.

Sheena Elizabeth Radford FRS FMedSci is a British biophysicist, and Astbury Professor of Biophysics in the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology at the University of Leeds. Radford is the Associate Editor of the Journal of Molecular Biology.

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Rajesh Vasantlal Thakker is May Professor of Medicine in the Nuffield Department of Clinical Medicine at the University of Oxford and a fellow of Somerville College, Oxford. Thakker is also a Consultant physician at the Churchill Hospital and the John Radcliffe Hospital, Principal investigator (PI) at the Oxford Centre for Diabetes, Endocrinology and Metabolism (OCDEM) and was Chairman of the NIHR/MRC Efficacy and Mechanism Evaluation (EME) Board until Spring 2016.

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References

  1. 1 2 "Professor David Ron FMedSci FRS". London: The Royal Society. Archived from the original on 5 August 2014.
  2. 1 2 "Professor David Ron FRS FMedSci". London: The Academy of Medical Sciences. Archived from the original on 11 October 2014.
  3. "Scopus preview - Ron, David - Author details - Scopus". www.scopus.com. Retrieved 27 August 2021.