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Publication Date

Summer 2011

Degree Type

Thesis - Campus Access Only

Degree Name

Master of Science (MS)

Department

Biological Sciences

Advisor

Brandon White

Keywords

MAML1, Mastermind-Like Protein Family, Notch Signaling, Proteasomal degradation, Uniquitination

Subject Areas

Biology; Molecular biology; Cellular biology

Abstract

Notch signaling plays a crucial role in cell development and proliferation. The Notch receptor is an inducible transcription factor found on the cell surface. Upon interaction with its ligand, the Notch receptor is cleaved, releasing the Notch Intra-cellular Domain (NICD), which enters the nucleus and complexes with CBF1 and Mastermind (MAML1) to activate target genes. MAML1 is also involved in many other cell signaling pathways independently of Notch signaling. In this study, we focused on determining whether MAML family members follow the same path as the Notch intra-cellular domain, which undergoes ubiquitination and degradation via the ubiquitin-proteasome pathway. We also examined the regions of MAML1 required for ubiquitination and the kinase(s) that may be involved in phosphorylation of MAML1. We determined that MAML1 was ubiquitinated as the shortest-lived family member and that the (75-300) amino acid region of MAML1 is essential for ubiquitination and degradation of MAML1. We also found MAML2, which is not ubiquitinated, to be the most stable member of the family.

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