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Home » Imaging-based Research » Yair Argon
Imaging-based Research
49 16Yair Argon, Ph.D.
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- Immunology 6a
- Pharmacology 6b
- Cell and Molecular Biology e
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43 3615 Civic Center Boulevard
Philadelphia, PA 19104-4318
34 Fax: (267) 426-5165
34 Lab: (267) 426-5130
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21 9 B.S. 14 (Biology) c
52 The Hebrew University Medical School, Jerusalem, Israel , 1974.
21 a Ph.D. 19 (Biochemistry) c
2f Harvard Medical School, 1980.
21 b Fellow 1e (Molecular Biology) c
57 Medical Research Council Lab of Molecular Biol., Cambridge, UK, 1984.
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Description of Penn IMIG Expertise
34Research:
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B and T lymphocytes, dendritic cells and macrophages sense their environment using a number of cell-surface receptors, and respond to environmental signals by secreting proteins that bind to infectious agents or to other immune system cells. Both the specificity of immune cells and their ability to act depend on proper expression of these membrane receptors and secreted proteins. All are multi-subunit proteins that fold and assemble in the endoplasmic reticulum and then traffic to their site of action. The control of folding, assembly and proper expression of proteins in immune cells is dependent on accessory proteins termed molecular chaperones. The roles of molecular chaperones, in particular, the role of GRP94, an essential ER stress protein, during the production of growth factors and differentiation of B cells is a major focus of research in the Argon lab. The lab uses microscopy to track antigen uptake by lymphoid cells, expression of surface proteins as well as ER dynamics under normal and stress conditions.
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Lab expertise and resources:
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- Live cell imaging of fluorescent fusion proteins
- Cells with depleted or increased expression of chaperones
- Chaperone knockout mice
- Molecular biology
- RNAi using viral vectors
- Biochemical analysis of proteins
- Proteomic methods
- Fluorescent ER stress reporters
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IMIG Collaborations:
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- Argon and Burkhardt: antigen presentation by dendritic cells
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Lab members:
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- Devin Dersh - Graduate student
10- ER quality control
- dcdersh@gmail.com
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f - Yina Dong - Research associate
10- IGF processing and signaling
- dongy@email.chop.edu
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f - Davide Eletto - Post-doctoral fellow
10- Cell-based assays, RNAi
- davide.laptop@gmail.com
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f - Jose James
14 - Technician
e- jamesjk@email.chop.edu
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f - Michal Marcez - Senior research associate
10- IGF signaling, tumor progression
- mimarzec73@gmail.com
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f - Olga Ostrovsky - Research associate
10- md88olga@yahoo.com
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Selected Publications
115 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. Nat. Acad. Sci 106(28): 11600-5, 2009 PMCID: PMC2710619.120 Ostrovsky O, Ahmed NT, Argon Y: The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation. Mol. Biol. Cell 20(6): 1855-64, 2009 PMCID: PMC2655248.
f4 Biswas C, Ostrovsky O, Makarewich CA, Wanderling S, Gidalevitz T, Argon Y.: The peptide binding activity of GRP94 is regulated by calcium Biochem. J 405(2): 233-41, 2007.
11e Wanderling S, Simen BB, Ostrovsky O, Ahmed NT, Vogen SM, Gidalevitz T, Argon Y.: GRP94 is essential for mesoderm induction and muscle development because it regulates IGF-II. Mol. Biol. Cell 18(10): 3764-75, 2007.
df Elkabetz Y, Argon Y, Bar-Nun S.: Cysteines in the CH1 domain underlie retention of unassembled Ig heavy chains. J. Biol. Chem 280(15): 14402-12, 2005.
fb 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 13(4): 433-442, 2000.
122 Dul JL1, 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 152(4): 705-16, 2001.
140 Davis DP1, Gallo G, Vogen SM, Dul JL, Sciarretta KL, Kumar A, Raffen R, Stevens FJ, Argon Y.: Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain. J. Mol. Biol 313(5): 1023-1036, 2001.
ff Vogen S, Gidalevitz T, Biswas C, Simen BB, Stein E, Gulmen F, Argon Y.: Radicicol-sensitive peptide binding to the N-terminal portion of GRP94. J. Biol. Chem 277(43): 40742-50, 2002.
129 Gidalevitz T, Biswas C, Ding H, Schneidman-Duhovny D, Wolfson HJ, Stevens F, Radford S, Argon Y.: Identification of the N-terminal peptide binding site of glucose-regulated protein 94. J. Biol. Chem. 279(16): 16543-52, 2004.
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