Deepa Dabir, professor of biology at Loyola Marymount University, is currently investigating “Aim32, a Multi-faceted Redox Protein, in Mitochondrial Biogenesis” thanks to $431,700 in grant funding awarded to her by the National Institutes of Health – General Medical Sciences Institute.
AIM32 is a more recently identified protein in the mitochondria. Mitochondria are organelles within cells that primarily function as the “powerhouses” of the cell by converting food into energy. Scientists often call mitochondria the powerhouses of the cell, because they produce about 90% of the energy that cells need to function. Mitochondrial biogenesis is the complex cellular process of generating new mitochondria or increasing mitochondrial mass, essential for replacing damaged organelles and maintaining cell energy balance. Since mitochondria play a role in so many of the human body’s processes, it is believed they may also contribute to the development of many diseases and disorders.
Dabir’s research focuses on aspects of mitochondrial biogenesis that include the characterization of the mitochondria’s protein import pathways, the impact of mitochondrial thioredoxin-like ferredoxin proteins to physiology, and mitoribosome assembly, which is the complex and highly coordinated process of building the protein-making machines inside the mitochondria. This research is integral to understanding how defects in mitochondrial biogenesis lead to disease, as well as how effective treatments for mitochondrial disorders might be developed.
Dedicated to bettering public health through her work, Dabir takes every opportunity to integrate undergraduate studies with hands-on research where she trains and guides the next generation of biologists and educators. She has engaged a total of six undergraduate and graduate students at Seaver College of Science and Engineering as part of her current research team. The model system being used for this research is yeast; a lot of the mechanisms and pathways are similar between yeast and mammalian systems. “All the biochemical studies that we envision performing as part of this research are integral to our understanding of mitochondrial biogenesis in yeast, but with direct application to mammals,” Dabir said.
The broad question they seek to answer through their research is “How does AIM32 contribute to proper mitochondrial and overall cellular function?’’ More specifically this NIH grant will enable them to address questions such as: 1) What are the mechanisms by which AIM32 is controlling cellular respiration, and does lack of AIM32 in the mitochondria cause less energy production? 2) Dabir’s previous research uncovered that AIM32 is present in the two largest compartments of the mitochondria – the matrix and the intermembrane space. So, the multi-part question here is: Are the functions of the AIM32 protein distinctive within each of these two compartments or are they overlapping? If this protein is removed from one compartment, but it is present in the other compartment, are some functions disrupted?
“What I’m aspiring to do is understand what normal mitochondrial physiology looks like,” said Dabir. “As we identify new proteins in the mitochondria [such as AIM32] and figure out their functions, we come to realize that mitochondrial physiology is complex and there are a lot of ‘players’ controlling it. Once we clarify or shed light on how things are regulated, we hope to gain a clearer understanding of what might be going wrong under conditions of disease.”
This new research revolves around understanding more about function of AIM32. “My first NIH grant research, started in 2019, alluded to the roles or functions AIM32 might be playing in the mitochondria,” Dabir explains. “With this three-year grant awarded in late 2024, my research team is taking a deeper dive to establish mechanisms for how AIM32 might perform different roles in the mitochondria.”
An overview of Dabir’s 2019 NIH grant research is available here.
