Walter K. Schmidt, Ph.D.
Associate Professor
Complete CV

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

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

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

The CaaX Proteases: Rce1p is an ER membrane-localized protease of unknown mechanism. This protease is essential for the maturation of isoprenylated molecules that are involved in cellular transformation (e.g., Ras and RhoB). We aim to understand the proteolytic mechanism of Rce1p and to develop pharmacological inhibitors that have anti-tumor potential. Rce1p has partial overlapping function with the ER membrane-localized, the zinc-dependent Ste24p protease, which has been linked to premature aging (progeria) because of its role in lamin A production. Thus, we are also trying to understand the functional differences of Rce1p and Ste24p to better understand their relative physiological importance.

The M16A Proteases: Ste23p and Axl1p are zinc-dependent metalloproteases that are required for the maturation of the isoprenylated yeast a-factor mating pheromone. These proteases are part of the M16A subfamily of metalloproteases, which 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.