Type of Thesis
Molecular, Cellular, & Developmental Biology
Loren Hough, Ph.D.
Jennifer Martin, Ph.D.
Nancy Guild, Ph.D.
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.
Rhoads, Caroline, "Investigations of Interactions between the Microtubule Binding Domain of Centrosomal P4.1 Associated Protein and Polyglutamylated Microtubules" (2018). Undergraduate Honors Theses. 1774.