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Examining the Potential Modification of the Protein Tyrosine Kinase Pyk2 by SUMO-1

  • Author / Creator
    Beatty, Jessica
  • Proline-rich tyrosine kinase 2 (Pyk2) is a non-receptor protein tyrosine kinase that is highly expressed in hematopoietic cells. Our lab generated two polyclonal antibodies to investigate the regulation of Pyk2 in macrophages and T cells. In macrophages the N-terminal antibody immunoprecipitated a higher molecular weight form of Pyk2. This shift was not due to differential phosphorylation or isoform expression. Since FAK, a close relative to Pyk2 undergoes a molecular weight shift due to SUMOylation, my thesis project was to investigate the potential SUMOylation of Pyk2. This study demonstrates that endogenous and exogenous Pyk2 associates with SUMO-1. The E3 ligase PIAS1 was shown to promote the association of Pyk2 with SUMO-1. Lysines 35, 145, and 646 were not the sites of Pyk2 SUMOylation, although SUMO-1 does associate with Pyk2 in the FERM domain. Direct Pyk2 SUMOylation was not confirmed, although SUMO-1 and PIAS1 overexpression increases Pyk2 protein levels.

  • Subjects / Keywords
  • Graduation date
    2013-11
  • Type of Item
    Thesis
  • Degree
    Master of Science
  • DOI
    https://doi.org/10.7939/R3SN01C59
  • License
    This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.
  • Language
    English
  • Institution
    University of Alberta
  • Degree level
    Master's
  • Department
    • Department of Medical Microbiology and Immunology
  • Specialization
    • Immunology
  • Supervisor / co-supervisor and their department(s)
    • Ostergaard, Hanne (MMI)
  • Examining committee members and their departments
    • Magor, Kathy (MMI)
    • Ingham, Rob (MMI)
    • Smiley, Jim (MMI)