K847A Mutation and Anionic Lipid-Presence Modify Opa1 Enzyme Kinetics and Function

Authors

J. Rafael Tolentino, DePauw University
Kate Walsh, DePauw University
Andrew D. Kehr, DePauw University

Files

Document Type

Poster

Publication Date

10-1-2025

Abstract

Opa1 is a dynamin superfamily protein that is responsible for the fusion of the mitochondrial membrane. However, nobody knows the specific chemical mechanisms of how it interacts with lipids. Our research focuses on investigating how Opa1 interacts with lipids. In other words, we want to figure out which amino acids are crucial for Opa1's ability to bind with lipids. In hopes of understanding how Opa1 mutations affect neurodegenerative diseases, such as dominant optic atrophy.

Department

DePauw University School of Liberal Arts and Sciences, Department of Chemistry and Biochemistry

Project Mentor

Andrew Kehr

Funding and Acknowledgements

Asher Student-Faculty Research Fund

Recommended Citation

Tolentino, J. Rafael; Walsh, Kate; and Kehr, Andrew D., "K847A Mutation and Anionic Lipid-Presence Modify Opa1 Enzyme Kinetics and Function" (2025). Annual Student Research Poster Session. 212.
https://scholarship.depauw.edu/srfposters/212