In This Section

Yair Argon, PhD
Yair Argon
Professor of Pathology and Laboratory Medicine

Dr. Argon investigates the unfolded protein response (UPR) , an essential signaling network that determines life or death of stressed cells and tissues. The IRE1 sensor of UPR responds to metabolic stress through four distinct activities and he focuses on determining which stress condition induces each activity and how they are integrated to enable the cells to cope with stress.



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Dr. Argon's recent research focus on the induction of the unfolded protein response (UPR) during cell differentiation charts a full scientific circle, as he started his independent research program defining the UPR phenomenon. His research now focuses on the role of UPR in combating diseases like diabetes and growth retardation.

Much of Dr. Argon's research program concerns the control of protein folding in the endoplasmic reticulum by molecular chaperone and the challenge of quality control of the secretory proteome.

Education and Training

BS, Hebrew University Medical School (Biology), 1974

PhD, Harvard University Medical School (Biochemistry), 1980

Fellowship, Medical Research Council Lab of Molecular Biology, Cambridge (Molecular Biology), 1984

Titles and Academic Titles

Professor of Pathology and Laboratory Medicine

Professional Awards

Young Investigator Award, Arthritis Foundation, 1986-1989

Junior Faculty Research Award, American Cancer Society, 1988–1991

Publication Highlights

Eletto Dav., Eletto Dan., Dersh D, Gidalevitz T, Argon Y. Protein Disulfide Isomerase A6 controls the decay of IRE1α signaling via disulfide-dependent association. Mol Cell. 2014 Feb; 53(4):562-576. PMID: 24508390
Ostrovsky O, Makarewich CA, Snapp EL, Argon Y. An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells. Proc Natl Acad Sci U S A. 2009 Jul; 106(28):11600-5. PMID: 19553200
Ostrovsky O, Ahmed NT, Argon Y. The Chaperone Activity of GRP94 Towards Insulin-like Growth Factor II Is Necessary for the Stress Response to Serum Deprivation. Mol Biol Cell. 2009 Mar; 20(6):1855-64. PMID: 19158397
Dul JL, Davis DP, Williamson EK, Stevens FJ, Argon Y. Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains. J Cell Biol. 2001 Feb; 152(4):705-16. PMID: 11266462
Davis PD, Raffen R, Dul LJ, Vogen MS, Williamson KE, Stevens JF, Argon Y. Inhibition of amyloid fiber assembly by both BiP and its target peptide. Immunity. 2000 Oct; 13(4):433-42. PMID: 11070162