Document Type

Thesis

Date of Degree Completion

Spring 2015

Degree Name

Master of Science (MS)

Department

Chemistry

Committee Chair

Todd Kroll

Second Committee Member

Carin Thomas

Third Committee Member

Holly Pinkard

Abstract

Lhx2 is a protein that is expressed in a gradient across the developing neocortex and is involved in arealization, the process through which this structure is divided into functional fields. However, little is known on how Lhx2's graded expression across the neocortex actually regulates the locations and sizes of the neocortical areas. In an attempt to understand how Lhx2 performs its functions within the neocortex, a yeast two-hybrid screen was used to identify possible binding partners for Lhx2. Of the sixteen pulled from the screen, two proteins, Eri3 and Ddx50, were deemed as having the highest likelihood of playing a role in neocortical arealization. The full length open reading frames of these two proteins were cloned and used for additional yeast two-hybrid assays to confirm whether they interact with Lhx2. These assays determined that Eri3 interacts with the Lim domain of Lhx2, while the Lhx2-Ddx50 interaction remains unconfirmed.

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