Publication Date

2021

Document Type

Dissertation/Thesis

First Advisor

Devergne, Olivier

Degree Name

M.S. (Master of Science)

Legacy Department

Department of Biological Sciences

Abstract

The abundant epithelial cells play various roles in the development and maintenance of an organism, and their apical-basolateral polarity is a unique characteristic that is imperative to their function and integrity. This polarity is maintained via various environmental cues and tightly regulated intracellular trafficking, where the presence of the basement membrane (BM) provides a basal cue. The BM is a specialized extracellular matrix (ECM) secreted by the epithelial cells, which accumulates on the basal side and serves as their mechanical anchorage. Although the BM is of paramount importance in the apical-basolateral polarity and the loss of BM’s integrity is a hallmark of cancer, little is known regarding the basal deposition restriction of BM components. Crag is a regulator of the biological pathway dedicated to the basal restriction of BM components, however, its interactors and the exact mechanism responsible for its polarized intracellular localization and its activity remain yet to be elucidated. In this thesis, a structure-function analysis of Crag was performed using the follicular epithelium (FE) of the Drosophila melanogaster ovary as the model system to determine the specific Crag’s domain(s) responsible for localization and activity. In this multidomain protein, we determined that the CBS domain plays an important role in the localization of Crag to the apical and lateral domains, and the DENN domains play a role in the activity of Crag in restricting BM components to the basal side. These results allowed us to begin to understand which domains of Crag are important for its localization and its activity of regulating the polarized deposition of BM protein. Next, we will continue this structure-function analysis of Crag to precisely determine the relative importance of each of the domains present in its localization and activity. Overall, this study will help us to further understand how Crag works in the biological pathway that regulates the polarized deposition of BM proteins.

Extent

115 pages

Language

eng

Publisher

Northern Illinois University

Rights Statement

In Copyright

Rights Statement 2

NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.

Media Type

Text

Download

Share

COinS