Proteins and protein-complexes underlying mitochondrial structure-function and metabolism: implications in diseases

The mitochondrial proteome plays a pivotal role in maintaining cellular health and function. The human MitoCarta3.0 dataset has curated 1136 proteins with mitochondrial localization primarily determined through mass spectrometry of mitochondria isolated from fourteen tissues and assessment of protein localization via large-scale green fluorescence protein tagging followed by microscopy (Rath et al., 2020). Many of these proteins are integral components of large complexes that control various aspects of mitochondrial functions. Some examples of these complexes, regulating crucial mitochondrial functions, include Oxidative phosphorylation (OXPHOS) complexes, mitochondrial permeability transition pore (mPTP), translocase complexes, pyruvate dehydrogenase complex, and mitochondrial ribosomes. While a significant number of mitochondrial proteins have undergone functional characterization, limited knowledge exists regarding their organization into complexes, stability, and dynamic assemblies under varying cellular physiological conditions.