Characterization of Transforming Acidic Coiled Coil Protein Three, a Protein Phosphatase One Binding Protein

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2018-01-08
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Abstract
Protein phosphorylation is a key signaling mechanism utilized by cells as a means of regulating various pathways within the cell. Protein phosphatase one (PP1) is a highly conserved enzyme that catalyzes the removal of a phosphate group from serine/threonine residues in eukaryotes. PP1 gains substrate specificity through the binding of regulatory proteins, of which over 200 are currently identified in humans. Most of these subunits dock PP1 via the RVxF binding motif. Transforming acidic coiled coil protein three (TACC3) has been identified as a potential PP1 interactor through quantitative mass spectrometry and also contains an RVxF motif (KVTF). Here, I have validated the TACC3-PP1 interaction, and demonstrated that it occurs via the RVxF motif. TACC3 is a non-motor spindle assembly protein and plays an important role in the proper segregation of chromosomes during mitosis. Due to its key role in maintaining genomic integrity, it has recently been implicated in a number of cancers. Here, I explore the expression of TACC3 mRNA in 20 cancers and the effect of aberrant TACC3 expression on patient survival from clinical data. The work presented here increases our knowledge of PP1 and its interaction with the regulatory subunit TACC3, and also provides insight into the role TACC3 is playing in cancer.
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Rackel, B.D. (2017). Characterization of Transforming Acidic Coiled Coil Protein Three, a Protein Phosphatase One Binding Protein (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca.