Biology Department |
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Biology Department |
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Dr. Ardythe A. McCrackenProfessor
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University of Delaware, Newark, DE
1976, M.S. Biology-Cytogenetics,
University of Delaware, Newark, DE
1981, Ph.D., Molecular Biology-Genetics
University of Colorado Health Sciences Center, Denver, CO
1981 - 1983 Postdoctoral Training, Protein Biochemistry and
Secretion
University of Colorado Health Sciences Center, Denver, CO
1983 - 87 Assistant Professor, Dept. Biochem/Biophys/Genetics
University of Nevada, Reno, NV
1987 – 1998 Assistant & Associate Professor, Department
of Biology
University of Nevada, Reno, NV
1998 - present Professor, Department of
Biology
Recently, I have been teaching a Biology Major's core course, BIOL 315 - Cell Biology, for students concentrating in Cell and Molecular Biology. The course enrollment typically includes biology, biochemistry, and pre -health majors. I also teach a graduate level course CMB 710 - Molecular Cell Biology, for first year graduate students in the CMB, Biochemistry, and CMPP graduate programs. In addition, I am frequently the instructor for the BIOL 495/695 seminar series and have taught Genetics, Human Genetics, and Introductory Biology in past years at the University of Nevada. My teaching responsibilities also include instruction and training of advanced undergraduate and graduate students in my research laboratory.
My research interests include the molecular biology of intracellular protein trafficking and the underlying common principles and mechanisms, with emphasis on events of the secretory pathway. Our current work is focused on understanding a quality control process that ensures nascent proteins are correctly folded, processed, and completely assembled before they exit the endoplasmic reticulum (ER) for further transport through the secretory pathway. Most proteins that fail to pass this checkpoint are degraded. The process by which these aberrant and unassembled secretory proteins are removed from the ER is referred to as ER-associated protein degradation, or ERAD. A unique aspect of ERAD uncovered by our studies is that ER-lumenal protein substrates are exported to the cytoplasm for degradation by the proteasome complex. This discovery has far reaching significance in that it reveals a cellular function for a retrograde protein transporter in the ER, a mechanism implicated in the delivery of cytotoxic proteins to the cytoplasm of the cell, and a transport pathway exploited by the human cytomegalovirus to mask its presence in infected cells. Experimental approaches used in my laboratory include: a.) traditional mutagenesis and genetic techniques with yeast and mammalian cells to identify the cellular components involved in the secretion pathway; b.) genetic engineering of secretion defective mutants through heterologous gene expression, to study protein determinants required for normal secretion; and c.) cell free systems which reconstitute cellular processes such as ERAD, to determine what molecules and mechanisms are involved.
Brodsky, J.L. and McCracken, A.A. 1997. ER-Associated Degradation and the Proteasome; How Topologically Restricted Events Came Together. Trends Cell Biol. 7:151-155.
McCracken, A.A., Werner, E.D., and Brodsky, J.L. 1998. ER-Associated Protein Degradation: An Unconventional Route to a Familiar Fate. In, Advances in Molecular Cell Biology: Intracellular Protein Degradation. Ed., A.J. Rivett, JIA press Inc., Stamford, Conn. Volume 27:165-200.
Brodsky, J.L, Werner, E.D., Dubas, M. E , Kruse, K.B., and McCracken, A.A.,., 1999. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274:3453-60
Brodsky, J.L. and McCracken, A.A. 1999 ER Protein Quality Control and Proteasome-Mediated Protein Degradation, Seminars in Cellular and Developmental Biology 10:507-513.
McCracken, A.A, Werner, E.D, Powel, M.L , Kruse, K.B., and Jeffery Brodsky. 2000. Differential Fates of Mutant Invertases in the Yeast ER. Yeast 16:1-7.
McCracken, A. A. and J. L. Brodsky. 2000. A molecular portrait of the response to unfolded proteins. Genome Biology 1: 1013.1-1013.3
McCracken, A. A. and J. L. Brodsky. 2001 Protein Export from the Endoplasmic Reticulum to the Cytosol: Methods "Encyclopedia of Life Sciences" www.els.net http://www.els.net/els/els/els/index.html?sessionid=cd80d8f0210c997c
Zhang, Y., G. Nijbroek, M. L. Sullivan, A. A. McCracken, and J. L. Brodsky. 2001 The Hsp70 molecular chaperone facilitates the ER associated degradation of the Cystic Fibrosis Transmembrane Conductance Regulator in yeast. Mol. Biol. Cell 12:1303-1314
Palmer, E. A., K. B. Kruse, and A. A. McCracken. 2001 A yeast expression vector and LEU2 selection in E. coli. PLASMID 46:57-59.
Lee RJ, C. Lin, C. Harty, A. A. McCracken, K Romish, GN DeMartino, PJ Thomas, & JL Brodsky. 2002. The 19S (PA700) cap of the 26s proteasome is sufficient to retrotranslocate and deliver a soluble polypeptide for ER associated Degradation (ERAD). EMBO, in press.
Palmer, EA, Kruse, KB, Buchannan, SM, Brodsky, JL, and McCracken, AA. 2002. J. Cell Science, in revision.
Street address
University of Nevada
Biology Department m/s 314
Reno NV 89557
Electronic mail address
mccracke@unr.edu
Web address
http://www.scsr.nevada.edu/~bioweb/biology/am.html
Office phone
775-784-6188
FAX number
775-784-1650
University of Nevada, Reno
Please Direct Questions to: biology@.unr.nevada.edu
