Submission Date

7-19-2019

Document Type

Paper- Restricted to Campus Access

Department

Biology

Faculty Mentor

Rebecca Lyczak

Comments

Presented during the 21st Annual Summer Fellows Symposium, July 19, 2019 at Ursinus College.

This project was supported by a National Institutes of Health Academic Research Enhancement Award (AREA) grant (1 R15 GM110614-02).

Project Description

The nematode worm Caenorhabditis elegans are model organisms commonly used to study development due to their transparency and quick reproductive cycle. Their genome is well-studied, and they have sophisticated processes that can potentially shed light on biological functions in humans. The actomyosin cytoskeleton of C. elegans is made up of actin proteins that dynamically control the movements of the cell along the outer edge, also known as the cortex. Cytoskeletal regulators and protein networks are important to coordinate antero-posterior polarity and cytokinesis (cell division). We study pam-1 mutants that have defects in this protein network. Mutant cells show misregulation of the cortical cytoskeleton and show blebbing defects due to increased cortical activity. We are currently working to figure out how PAM-1 interacts with cytoskeletal proteins in regulating cortical dynamics. Two proteins we are studying are ANI-1, an important protein in remodeling the actin cytoskeleton and moesin, a membrane linker for cortical F-actin. Gene expression can be inactivated through the technique RNA interference. This bacterial feeding method knocks out gene function, specifically ani-1, which is used in examining its role during first division by observing phenotypes in wildtype and pam-1 mutant worms. The worms are imaged at the single cell embryo stage with DIC microscopy until the completion of cytokinesis. Confocal microscopy of moesin tagged with GFP is used for studying protein localization and in visualizing the actin network during cytokinesis. These two methods help in understanding the required cytoskeletal components in the observed phenotypes of pam-1mutants.

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