Document Type

Thesis

Date of Degree Completion

Fall 2019

Degree Name

Master of Science (MS)

Department

Chemistry

Committee Chair

Todd Kroll

Second Committee Member

Carin Thomas-Bradley

Third Committee Member

April Binder

Abstract

The neocortex of the mammalian brain is allocated into specialized areas during embryonic development. In mice, as well as humans, the neocortex develops four primary areas: somatosensory, auditory, visual, and motor. In the adult neocortex, the boundaries between these four areas are marked by differences in cellular architecture and gene expression patterns. However, these physical boundaries are not evident during embryonic development of this structure. Rather, the neocortex initially appears uniform across its expanse, with one exception: a handful of proteins that regulate neocortical arealization are generated in gradients across the expanse of the neocortex and control the size of the future neocortical areas. The most highly characterized protein involved in this process is Emx2. Previous researchers in our lab have identified two Emx2-interacting proteins, Cnot6l and QkI (which exists in three forms) that interact with each other. These interactions were initially identified by a yeast two-hybrid screen and then confirmed by pull-down assays. The goal of this project is to use GST pull-down assays determine whether or not various combinations of these five proteins can interact to form a larger complex. The results indicate that larger protein complexes can be formed between Emx2 with Cnot6l and any of three QkI isoforms, as well as larger complexes are formed with Emx2 and any combination of two of the three QkI proteins. The QkI isoforms can also form larger complexes with each other and with Emx2 and Cnot6l. However, it was determined that QkI-6 and QkI-7 may or may not interact with QkI-5 and Cnot6l simultaneously. These results are inconclusive due to the two proteins only differing by six amino acids and overlapping of the two proteins on the resulting western blots.

Included in

Biochemistry Commons

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