Welcome to
The Schmidt L
ab

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Schmidt Lab Alumni

Walter K. Schmidt, Ph.D.
Associate Professor

BA , Rice University, 1989
PhD, UC-Berkeley, 1995
PostDoc, Johns Hopkins SOM, 1995-2001

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

UGA Affiliations
Integrated Life Sciences

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

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

Community Info
Biomedical Research in Georgia
Athens Area Visitors Guide
Athens-Wikipedia

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WANTED: New students willing to tackle challenging and interesting basic science problems related to human disease (e.g. cancer, aging, and prions).

OUTCOMES: Past lab members have leveraged their training for great positions: click here.

Our lab uses a variety of technical approaches to better understand how post-translational modifications regulate the function of CaaX-type proteins. These proteins are subject to an ordered series of C-terminal modifications: isoprenylation, proteolysis, and carboxylmethylation (steps 1-3 in figure below). Prominent examples of CaaX proteins are the Ras family of oncoproteins, Ras-related proteins, kinases, fungal mating pheromones, and Hsp40 chaperones, among others.

The Shunt Pathway: We recently discovered that CaaX proteins do not always follow the standard modification pathway. Some follow an isoprenylation-only branch that we call the shunt pathway (see branch after step 1 in figure below). We hypothesize that CaaX proteins have a strong preferenence for either the standard or shunt pathway. We are testing our predictions by determining the preffered modification pathway of CaaX protein reporters and detailing the consequences of altered pathway selection. Effects observed range from altered protein function / localization to changes in cellular phenotypes.

The CaaX Proteases: Rce1p and Ste24p are ER membrane-localized proteases. Our research on the proteolytic mechanisms, substrate profiles, and inhibitors of these proteases is expected to guide therapeutic strategies (e.g. cancer treatments). We also expect to gain a better understanding of how they function as gatekeepers for entry into the standard pathway.

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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