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Imaging-based Research

Yair Argon, Ph.D.

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Professor of Pathology and Laboratory Medicine
Department: Pathology and Laboratory Medicine

Contact information
816 Abramson Research Center
3615 Civic Center Boulevard
Philadelphia, PA 19104-4318
Office: (267) 426-5131
Fax: (267) 426-5165
B.S. (Biology)
The Hebrew University Medical School, Jerusalem, Israel , 1974.
Ph.D. (Biochemistry)
Harvard Medical School, 1980.
Fellow (Molecular Biology)
Medical Research Council Lab of Molecular Biol., Cambridge, UK, 1984.
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> Perelman School of Medicine   > Faculty   > Details

Description of Penn IMIG Expertise


Argon Reserach PhotoB 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.

Lab expertise and resources:

  • 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

IMIG Collaborations:

  • Argon and Burkhardt: antigen presentation by dendritic cells

Lab members:

Selected Publications

Ostrovsky, O,C. Makarewich, E.L. Snapp. and Y. Argon: An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells. Proc. Nat. Acad. Sci. Page: 106(28):11600-5. 2009 PMCID: PMC2710619.

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. 20(6): 20(6):1855-64. 2009 PMCID: PMC2655248.

Biswas, C., Ostrovsky, o., Makarewich, C.A., Wanderling, S., Gidalevitz, T., and Argon, Y.: The peptide binding activity of GRP94 is regulated by Calcium Biochem. J. Page: 405(2):233-41. 2007.

Wanderling, S., Simen, B.B., Ostrovsky,O., Ahmed,N.T., Vogent, S.M., R. Gidalevitz, and Y. Argon: GRP94 is essential for mesoderm induction and muscle development because it regulates IGF-II. Mol. Biol. Cell. Page: 18(10):3764-75, 2007.

Elkabetz, Y., Argon, Y., Bar-Nun, S.: Cysteines in the CH1 domain underlie retention of unassembled Ig heavy chains. J. Biol. Chem. Page: 280(15):14402-12, 2005.

Davis, P.D., Raffen, R., Dul, J. L., Vogen, S., Williamson, E.K., Stevens, F.J., Argon, Y.: Inhibition of amyloid fiber assembly by both BiP and its target peptide. Immunity Page: 13(4):433-442, 2000.

Dul, J.L., Davis, P. D., Williamson, E.K., Stevens, F.J., Argon, Y.: Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains. J. Cell. Biol. Page: 152(4):705-16. 2001.

Davis, D.P., Gallo, G., Vogen, S.M., Dul, J.L., Sciarretta, K.L., Kumar, A., Raffen, R., Stevens, F.J., Argon, Y.: Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain. J. Mol. Biol. 313: 313(5):1023-1036, 2001.

Vogen, S.M., Gidalevitz, T., Biswas, C., Simen, B.S., Stein, E., Gulmen, F., Argon, Y.: Radicicol-sensitive peptide binding to the N-terminal portion of GRP94. J. Biol. Chem. Page: 277(43):40742-50, 2002.

Gidalevitz, T., Biswas, C., Ding, H., Schneidman-Duhovny, D., Wolfson, H.J., Stevens, F., Radford, R., and Argon, Y.: Identification of the N-terminal peptide binding site of glucose-regulated protein 94. J. Biol. Chem. Page: 279(16):16543-52, 2004.

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Last updated: 04/01/2016
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