Submission Date

7-19-2023

Document Type

Paper- Restricted to Campus Access

Department

Biology

Faculty Mentor

Rebecca Lyczak

Comments

Presented during the 25th Annual Summer Fellows Symposium, July 21, 2023 at Ursinus College.

This research was conducted at Ursinus College during Summer Fellows 2023 under the direction of Dr. Rebecca Lyczak. Funding for this research was provided by the National Institute of Health, grant R15GM110615.

Project Description

Caenorhabditis elegans are transparent nematodes often used as model organisms. Their fully sequenced genome, simple organ systems, and high fecundity make them ideal for studying protein interactions. PAM-1 is a puromycin sensitive aminopeptidase that acts as a cell cycle regulating protein. Specifically, PAM-1 regulates oocyte maturation and polarity establishment. Mutations in the pam-1 gene cause infertility, defects in polarity establishment, and abnormal progressions of meiosis and mitosis. The mechanisms through which these phenotypes are produced remain unclear. PAM-1 is of interest because puromycin sensitive aminopeptidases are highly conserved across the animal phylum, but how they function remains unclear. In humans, PAM-1 is homologous to a puromycin sensitive aminopeptidase called the NPEPPS protein. This protein is believed to play a protective role in neurological diseases such as Alzheimer’s disease. This summer I have been investigating protein interactions between PAM-1 and other proteins involved in oocyte maturation and embryogenesis in wildtype worms and pam-1 mutants via RNA interference and Western blots. Two specific proteins I am investigating are CDC-25.1 and MBK-2. CDC-25.1 dephosphorylates the maturating promoting factor in C. elegans oocytes, allowing oocytes to mature and become fertilized. Phosphorylation of the Minibrain kinase 2 (MBK-2), homologous to human dual-specificity tyrosine phosphorylation kinase 2 (DYRK2), is required for proper meiotic cell cycle progression in C. elegans. I am interested in investigating whether PAM-1 interacts with either of these proteins. If so, this would propose an explanation as to why the phenotypes seen in pam-1 mutants are observed.

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