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Signaling networks have emerged as the underlying regulatory system by which the many biological pathways required for sustaining life are coordinated. My laboratory uses a combination of biochemistry and proteomic mass spectrometry to understand the signaling networks mediated by the ubiquitin family of small protein modifications. Specifically, we are examining the role of two members of this family, ubiquitin and SUMO, in regulating key nuclear processes. Importantly, the deregulation of these two modification systems has been linked to the pathogenesis of many diseases including cancer, neurodegenerative diseases, and immune system disorders. Ubiquitin is a 76 amino acid protein that regulates the abundance and activity of a large number of cellular factors through its covalent attachment to lysines in target proteins. The specificity of this modification system is generated by a large family of ubiquitin ligases, each of which target a specific set of substrates for modification. We are currently characterizing a subset of these ubiquitin ligases that have been implicated in tumorigenesis. Using a combination of proteomic and biochemical tools, we are identifying the substrates of these ligases and working to understand how altering the modification state of these substrates can influence tumor progression. SUMO is another member of the ubiquitin family of small protein modifiers that plays a critical regulatory role in a number of different biological processes. We previously developed a series of proteomic tools that enabled us to characterize different aspects of this signaling pathway. These findings form the basis for ongoing work in my laboratory aimed at understanding how SUMO-regulated protein networks influence chromatin structure, cell cycle progression and genome stability and how misregulation of this pathway can play a critical role in tumorigenesis.
Signaling networks have emerged as the underlying regulatory system by which the many biological pathways required for sustaining life are coordinated. My laboratory uses a combination of biochemistry and proteomic mass spectrometry to understand the signaling networks mediated by the ubiquitin family of small protein modifications. Specifically, we are examining the role of two members of this family, ubiquitin and SUMO, in regulating key nuclear processes. Importantly, the deregulation of these two modification systems has been linked to the pathogenesis of many diseases including cancer, neurodegenerative diseases, and immune system disorders. Ubiquitin is a 76 amino acid protein that regulates the abundance and activity of a large number of cellular factors through its covalent attachment to lysines in target proteins. The specificity of this modification system is generated by a large family of ubiquitin ligases, each of which target a specific set of substrates for modification. We are currently characterizing a subset of these ubiquitin ligases that have been implicated in tumorigenesis. Using a combination of proteomic and biochemical tools, we are identifying the substrates of these ligases and working to understand how altering the modification state of these substrates can influence tumor progression. SUMO is another member of the ubiquitin family of small protein modifiers that plays a critical regulatory role in a number of different biological processes. We previously developed a series of proteomic tools that enabled us to characterize different aspects of this signaling pathway. These findings form the basis for ongoing work in my laboratory aimed at understanding how SUMO-regulated protein networks influence chromatin structure, cell cycle progression and genome stability and how misregulation of this pathway can play a critical role in tumorigenesis.
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