Recombinant Human CRIF1 protein (His tag N-Terminus)

補足情報

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CRIF1 also known as CRIFone is a protein implicated in coordinating mitochondrial translation and metabolism. It has a molecular weight of approximately 33 kDa. The gene encoding CRIF1 is found in humans and is expressed in various tissues including liver heart and skeletal muscle indicating its significant role in energy-demanding tissues. CRIF1 localizes mainly in the mitochondrial inner membrane where it interacts with mitoribosomes to facilitate the synthesis and integration of respiratory chain complexes.

Biological function summary

CRIF1 functionally contributes to the mitochondrial protein synthesis machinery and is a part of the mitoribosome complex. It directly interacts with nascent polypeptide chains during mitochondrial translation ensuring proper insertion into the mitochondrial inner membrane. This interaction is essential for effective cellular respiration and ATP production. The protein further plays a role in maintaining mitochondrial structure and regulating cellular energy homeostasis by stabilizing key mitochondrial complexes particularly involved in oxidative phosphorylation.

Pathways

CRIF1 participates noticeably in the oxidative phosphorylation and mitochondrial biogenesis pathways. In these pathways CRIF1 ensures the proper assembly and maintenance of the electron transport chain complexes. It interacts with other mitochondrial proteins such as COX1 and ND1 integral parts of Complex IV and Complex I of the electron transport chain respectively. These interactions position CRIF1 as critical for efficient energy production and metabolic regulation.

CRIF1 has been linked to metabolic syndromes and neurodegenerative diseases. Its dysregulation can impact mitochondrial function leading to energy production deficits seen in disorders like mitochondrial myopathies and Parkinson's disease. CRIF1 interacts with proteins like Parkin known to be involved in mitochondrial quality control processes. Disruptions in CRIF1 function can exacerbate defects in mitochondrial maintenance and turnover contributing to disease pathogenesis.