Investigations of Interactions between the Microtubule Binding Domain of Centrosomal P4.1 Associated Protein and Polyglutamylated Microtubules

Undergraduate Honors Thesis

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Citeable URL: https://scholar.colorado.edu/concern/undergraduate_honors_theses/zg64tm29x

Abstract

Microtubules maintain particularly diverse and important functions within the cell despite being polymers made up of two highly conserved proteins: a- and b-tubulin. Some of these diverse roles are explained by the presence of post-translational modifications occurring on the C-terminal tail of tubulin proteins, primarily detyrosination, polyglutamylation and polyglycylation. Misregulation of C-terminal tail post-translational modifications are observed in disease phenotypes and may increase the risk of some forms of cancers; however, the role of these post-translational modifications is not well understood. Working towards a goal of designing in vivo methods to study specific post-translational modifications, this paper examines the specificity of the interaction between the microtubule binding domain of centrosomal P4.1 associated protein and polyglutamylated microtubules using co-sedimentation assays.

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