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Permanent link (DOI): https://doi.org/10.7939/R3SN01C59

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

Descriptions

Other title
Subject/Keyword
Pyk2
SUMO-1
PIAS1
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Beatty, Jessica
Supervisor and department
Ostergaard, Hanne (MMI)
Examining committee member and department
Smiley, Jim (MMI)
Magor, Kathy (MMI)
Ingham, Rob (MMI)
Department
Department of Medical Microbiology and Immunology
Specialization
Immunology
Date accepted
2013-08-15T12:16:11Z
Graduation date
2013-11
Degree
Master of Science
Degree level
Master's
Abstract
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.
Language
English
DOI
doi:10.7939/R3SN01C59
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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