Jon Huibregtse

Huibregtse, Jon
Professor in Molecular Genetics & Microbiology
Graduate Advisor, Cell and Molecular Biology Graduate Program

E-mail: huibreg@mail.utexas.edu

Website: http://www.biosci.utexas.edu/mgm/People/Faculty/profiles/?id=1595

Main Office: MBB 2.312
Phone: 232-7700

Mailing Address:
The University of Texas at Austin - ICMB
1 University Station A4800
2500 Speedway
Austin, TX 78712-1095

Graduate Students:

  • Dastur, Anahita
  • Durfee, Larissa
  • Kim, Hyung Cheol

    • Research Summary:
       The Huibregtse lab studies the biochemistry of the ubiquitin proteolysis system, a major pathway for degradation of proteins in eukaryotic cells. Our interest in this pathway arose from study of human papillomaviruses (HPVs) and their association with uterine cervical carcinoma, the second leading cause of cancer-related deaths among women worldwide. Characterization of the HPV E6 protein showed that it promotes cellular immortalization by stimulating the ubiquitination and degradation of p53, an important tumor suppressor protein. This has led to insights not only into how HPV-infected cells escape normal growth regulation, but also to the identification of a class of ubiquitin ligases, known as HECT E3s. Current projects focus on understanding the biochemical mechanism and regulation of HECT E3s, in both mammalian and yeast cells, as well as the role of the HPV E6 oncoprotein in carcinogenesis. We are also studying the conjugation pathway for ISG15, a ubiquitin-like protein that becomes conjugated to a set of cellular proteins following activation of type I interferon pathways. The goal is to understand the function of ISG15 conjugation in anti-viral responses and the biochemical effect of ISG15 conjugation on target proteins.
     
    Publications:
    Hsel, a component of the yeast Hrs-STAM uubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to contol sorting efficiency into multivesicular bodies (2007) Mol. Biol. Cell. 18, 324-35.
    Hepatitis C virus indiced, E6-AP-dependent degradation of the retinoblastoma protein (2007) PloS Pathogens
    The HPV E6 protein and E6AP in cervical cancer (2007)
    Regulation of catalytic activities of HECT ubiquitin ligases (2007) Biochem. Biophys. Res. Comm. 354, 329-333.
    The Deubiquitinating enzyme Ubp2 modulates Rsp5-depdnent Lys63-linked polyubiquitin conjugates in Saccharomyces cerevisiae (2006) J. Biol. Chem. 281, 36724-36731.
    Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells (2006) J. Biol. Chem. 281, 4334-4338.
    The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme (2005) EMBO Journal 24, 2414-2424.
    Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways (2005) Proc. Natl. Acad. Sci. USA 102, 10200-10205.
    The global transcriptional effects of the human papillomavirus E6 protein in cervical carcinoma cell lines are mediated by the E6AP ubiquitin ligase (2005) J. Virol. 102, 3737-3747.
    The E6AP ubiquitin ligase is required for transactivation of the hTERT promoter by the human papillomavirus E6 oncoprotein (2005) J. Biol. Chem. 280, 10807-10816.
    UPS shipping and handling (2005) Cell 120, 2-4.
    The -4 phenylalanine is required for substrate ubiquitination catalyzed by HECT ubiquitin ligases. (2004) J. Biol. Chem. 279, 18935-18943.
    The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, and IFN-alpha/beta-induced ubiquitin-like protein (2004) Proc. Natl. Acad. Sci. U.S.A. 101, 7578-7582.

     
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