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Radmila Sarac, Ph.D.
Office: Gyte 290
Telephone: (219) 989-2492
Email: saracr@calumet.purdue.edu |
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Education
B.S. Pharmacy, Purdue University, West Lafayette, IN
Ph.D. Neurobiology, Pharmacology, and Physiology, University of Chicago, Chicago, IL
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Research Interests
My primary research interests include understanding the functional and structural properties of the G protein-activated inwardly rectifying potassium ion channel (GIRK) family. GIRK channels are mediators of electrophysiological signals in the cell in addition to coupling to other biochemical signaling complexes. Inwardly rectifying potassium channels form heteromeric and homomeric channels, which are capable of assembly within a subfamily or less frequently, between subfamilies. GIRK subunits are differentially expressed and specific subunits have been shown to mediate diverse roles of channel targeting and expression. Utilizing multiple experimental methods to analyze protein expression, localization, and channel function, I have examined how different subunits of the GIRK channel contribute to functional properties, and specifically, which protein residues are involved in the activation and function of the assembled channel. Analysis of the specific mechanism of channel function is dependent upon not only the molecular composition of the channel, but also the diversity of expression, trafficking and interactions of the various subunits. For many proteins, specific molecular sequences have been identified that mediate interactions between proteins as well as the modification and targeting of the protein to the appropriate cellular environment, whether this results in export out of the ER or expression at the plasma membrane. Understanding how different GIRK subunits interact and dictate channel formation and localization will provide useful information when examining functional output of various systems coupled to the channel. In addition, crystallization of various bacterial potassium channels has provided a new basis of scientific knowledge in which to explore the relationship between protein architecture and possible contributions to function. The elucidation of channel function at a molecular level provides further information about protein and cellular mechanisms that mediate responses and contribute to a specific physiological role as well as possible roles in disease states. |
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Selected Publications:
(abstracts are linked to authors name, please click to view)
ChakrabartyT., Kambesis, N., Nelson D.J., and Sarac R.
Investigating hydrophobic domain interactions in G-protein
coupled inwardly rectifying potassium channels (GIRK) using
FRET microscropy. February 2006. Abstract. 50th Annual
Biophysical Society Meeting,
http://www.abstractsonline.com/viewer/SearchResults.asp
Sarac R, Hou P, Hurley, KM, Hriciste D, Cohen, N.A., and
Nelson DJ. Mutation of critical GIRK subunit residues
disrupts N and C termini association and channel
function.
J. Neuroscience. 2005, 25(7):1836-1846
Keshvara LM, Isaacson CC, Yankee TM, Sarac R, Harrison ML,
and Geahlen RL. Syk- and Lyn-Dependent Phosphorylation
of Syk on Multiple Tyrosines Following B Cell Activation
includes a Site that Negatively Regulates Signaling. The
Journal of Immunology 1998;161:5276-5283.
Drum CL, Yan S-Z, Sarac R, Mabuchi Y, Beckingham K,
Bohm A, Grabarek Z, Tang W-J. An Extended Conformation
of Calmodulin Induces Interactions between the Structural
Domains of Adenylyl Cyclase form Bacillus anthracis to
Promote Catalysis. The Journal of Biological Chemistry
2000;275(46):36334-36340.
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Courses
Bio 101 - Introductory Biology
Biol 214 - Anatomy and Physiology II |
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