Mark G. Goebl, Ph.D.

Professor of Biochemistry & Molecular Biology
Member of the Walther Oncology Center

Grant Support

Honors

Committees

Editorial Boards

Student Training

Memberships

Training

  • B.S., 1980: University of Notre Dame, South Bend, IN
  • Ph.D., 1985: University of Chicago
  • Post Doctoral, 1986-1989: University of Washington

Positions

  • Professor, 2000-present, Indiana University School of Medicine
  • Associate Professor, 1993-2000, Indiana University School of Medicine
  • Associate Member, 1989-present:  Walther Oncology Center, Indiana University School of Medicine, Indianapolis, IN
  • Assistant Professor, 1989-1993: Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN

Summary of the focus of the research of Dr. Goebl
We are using our knowledge of protein degradation to develop stable cell cycle inhibitors as anticancer therapeutics.

Description and summary of research focus of the laboratory:
Dr. Goebl's laboratory is interested in the regulation of the eukaryotic cell cycle by ubiquitin-dependent protein degradation. Progress through the cell cycle is controlled by protein kinases known as cyclin dependent protein kinases or CDKs. These CDKs are regulated by both activating subunits known as cyclins and inhibitory subunits known as CKIs. Both cyclins and CKIs are regulated at the level of protein degradation. That is, in order for cell cycle progression to occur, the proper cyclins must be stabilized and other cyclins and CKIs must be destroyed. These proteins are targeted for degradation by large complexes of proteins. These complexes add ubiquitin to the different cyclins and CKIs which allows these protein to be recognized by a protease known as the proteasome. A major focus of Dr. Goebl's laboratory is to identify the components of these complexes and to understand how their activities are regulated. These complexes are important for linking the control of cell cycle progression to growth control of the cell as well as differentiation. The cell also uses these protein complexes to control the amounts of cyclins and CKIs in response to cellular stresses such as DNA damage.

 

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