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)
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 can be found among the Ras family of oncoproteins that are often mutated in cancer.

Standard v. Shunt Pathway: We recently discovered that certain CaaX proteins follow an isoprenylation-only branch of the standard modification pathway that we refer to as the shunt pathway (e.g. see Ydj1p in figure below). Pathway preference appears linked to optimal CaaX protein function. We are determining the pathway followed by various CaaX protein reporters and detailing the consequences of altering their modification preference. These consequences range from altered protein activity, to differential localization, to changes in cellular phenotypes.

The CaaX Proteases: Rce1p and Ste24p are ER membrane-localized proteases. Our research centers on their proteolytic mechanisms, substrate profiles, and biological roles in the cell. We expect to gain a better understanding of their function as gatekeepers for CaaX protein modificaiton via the standard pathway and their utility as targets for disease therapy (e.g. cacner treatment).

The M16A Proteases: Ste23p and Axl1p are zinc-dependent metalloproteases that are part of the M16A subfamily of metalloproteases. They are related to 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 the largely uncharacterized M16 metalloprotease family as a whole, thus potentially providing novel insight into new methods for the treatment of AD and possibly other diseases.


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.

Other BCMB courses



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