Penn IMIG

Member Login ||

Imaging-based Research

Yair Argon, Ph.D.

faculty photo
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
Education:
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.
Permanent link
 
> Perelman School of Medicine   > Faculty   > Details

Description of Penn IMIG Expertise

Research:


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, 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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

back to top
Last updated: 03/21/2017
The Trustees of the University of Pennsylvania