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Research Interests
    Our recent studies have focused on the Snf1 kinase of yeast. The mammalian homologue of Snf1 is the AMP-activated protein kinase, an important therapeutic target for type II diabetes. Biochemical and genetic experiments have shown that Snf1 kinase is regulated by phosphorylation of the conserved threonine residue in the kinase activation loop. We have developed a phosphopeptide antibody that specifically recognizes the phosphorylated (active) form of Snf1 kinase. We have used the antibody to demonstrate that Snf1 is activated by three distinct upstream kinases called Sak1, Tos3 and Elm1. We would like to determine the mechanism by which glucose abundance determines the phosphorylation status of the Snf1 activation loop. Our most recent work has shown that the Snf1-activating kinases are not themselves regulated by glucose. Instead, it is the DEphosphorylation of the Snf1 activation loop that responds to changes in glucose abundance. Future studies will focus on understanding the molecular mechanisms regulating the dephosphorylation reaction.


    The long term goal of the lab is to identify all the components of the glucose signaling pathway in yeast and to understand how they interact in order to regulate gene expression and cellular metabolism. These studies will provide a better understanding of glucose-mediated regulation of cellular metabolism and have important implications for designing novel treatments for patients with diabetes.



 
Selected Publications
  1. Shirra,M.K., R.R. McCartney, C. Zhang, K.M. Shokat, M.C. Schmidt and K.M. Arndt (2008) "A Chemical-Genomics Study Identifies Snf1 as a Repressor of Gcn4 Translation" J. Biological Chemistry 283: 35889-35898. | Abstract

  2. Rubenstein, E.M., R.R. McCartney, C. Zhang, K.M. Shokat, M.K. Shirra, K.M. Arndt and M.C. Schmidt (2008) "Access Denied: Snf1 Activation Loop Phosphorylation is Controlled by Availability of the Phosphorylated Threonine 210 to the PP1
    Phosphatase" J. Biological Chemistry 283: 222-230. | Abstract

  3. Rubenstein, E.M. and M.C. Schmidt (2007) "Mechanisms regulating the protein kinases of Saccharomyces cerevisiae" Eukaryotic Cell 6:571-83 | Abstract

  4. Elbing, K., E.M. Rubenstein, R.R. McCartney and M.C. Schmidt (2006) "Subunits of the SNF1 kinase heterotrimer show interdependence for association and activity" J. Biological Chemistry 281:26170-26180 | Abstract

  5. Elbing, K., R.R. McCartney and M.C. Schmidt (2006) "Purification and Characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae"Biochemical Journal 393: 797-805 | Abstract



    Complete Publication Listing

  
 
Other Links
MGB Faculty Webpage
Schmidt Lab
University of Pittsburgh		  
   
     
  Martin Schmidt, Ph.D.
Office:  W1247 BST
Lab:W1212 BST
Phone:648-9243
mcs2@pitt.edu
 
Academic Affiliations
  • Director,
    Biochemistry and Molecular Genetics Program

  • Associate Professor,
    Department of Microbiology and Molecular Genetics

  • Member,
    Molecular Virology and Microbiology Program
 
Education
  • B.A. University of Vermont (1979)

  • Ph.D., University of California at Berkeley (1985)

  • Postdoctoral Fellow, University of Califormia at Los Angeles
 

 
 


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