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The Schmidt L

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Schmidt Lab Alumni

Walter K. Schmidt, Ph.D.
Associate Professor

Contact Information
A414B Life Sciences Building
University of Georgia
Athens, GA 30602
706-583-8241 (office), -8242 (lab)
706-542-1738 (fax)
Call/email to schedule appointment

UGA Affiliations
Department of Cellular Biology
Center for Metalloenzyme Studies
Biomedical and Health Sciences Institute
Fungal Molecular Biology Group
Developmental Biology Group
UGA Cancer Center

Other Affiliations / Links
Georgia Cancer Coalition
The International Protease Network
Saccharomyces Genome Database
Yeast in the Southeast

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About Our Research...
UGA Research Magazine (2003)
UGA Public Affairs (2005)
BHSI Newsletter (2005)
UGA Red&Black (2005)
UGA Columns (2006)
BHSI Newsletter (2008)

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In our lab, we use biochemical, cell biological, genetic, and molecular approaches in conjunction with the yeast system to better understand the impact of modifications associated with isoprenylated proteins. Examples of such proteins include the Ras family of oncoproteins, Ras-related proteins, kinases, secreted fungal mating pheromones, Hsp40 chaperones, and many others. Understanding the function of these modifications may lead to novel therapeutic strategies for cancer, Alzheimer's disease, progeria, and other diseases.

Novel Reporters:
Protein isoprenylation is a widespread modification that has been investigated using relatively few reporter proteins. We are developing new reporters to investigate the impact of modifications typically associated with this pathway.

The CaaX Proteases: Rce1p and Ste24p are ER membrane-localized proteases. Rce1p removes the last few amino acids of isoprenylated proteins that are involved in cellular transformation (e.g., Ras and RhoB). Ste24p is required for lamin A production and its dysfunction is linked to premature aging (progeria). Our research investigates the proteolytic mechanisms and substrate profiles of these proteases. This effort is expected to ultimately guide better therapeutic strategies (e.g. cancer treatments) and lead to a better understanding of their relative physiological importance in regulating the function of isoprenylated proteins.

The M16A Proteases: Ste23p and Axl1p are zinc-dependent metalloproteases that are part of the M16A subfamily of metalloproteases. The M16A family includes the insulin-degrading enzyme (IDE) that has a proposed protective function in Alzheimer's disease (AD). Our research on Ste23p and Axl1p is designed is to gain a better understanding of these largely uncharacterized yeast proteases and the M16 metalloprotease family as a whole, thus potentially providing novel insight into new methods for the treatment of AD.

The RAS Initiative: Want to learn more about Ras and therapeutic approaches aimed at interfering with Ras biology? The National Cancer Institute recently launched a national campaign to develop resources and new knowledge about Ras biology.

Course Related Information

FYOS 1001 resources - The Contributions of Underrepresented Minorities to Today's Understanding of Biology.

GRSC 8010 resources - Graduate Professional Development.

BCMB/CBIO/GENE 8212 resources - Comprehensive Graduate Course in Biochemistry, Molecular Biology, Cell Biology, and Genetics.

BCMB 8120 resources (class syllabus) - Advanced Topics in Gene Expression; click here to access the latest list of articles (make sure to refresh your browser).

Other BCMB courses

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