Anti-MRPL4 antibody [EPR13151]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

MRPL4 also known as 39S ribosomal protein L4 mitochondrial is a mitochondrial ribosomal protein. This protein is a component of the large 39S subunit of the mitochondrial ribosome and has a molecular mass of approximately 39 kDa. MRPL4 is primarily expressed in tissues with high energy demands including the heart and skeletal muscle. It plays a role in mitochondrial protein synthesis facilitating the translation of proteins encoded by mitochondrial DNA.

Biological function summary

MRPL4 assists in the assembly and stability of the mitochondrial ribosome forming part of the mitoribosome complex. This complex is essential for the synthesis of mitochondrial proteins which are critical for proper mitochondrial function. MRPL4 ensures accurate translation by binding to ribosomal RNA stabilizing the structure needed for efficient ribosomal activity. Its function is important for maintaining cellular energy production cellular growth and metabolism.

Pathways

MRPL4 participates significantly in the mitochondrial translation pathway. This pathway is integral to the oxidative phosphorylation process which is essential for ATP production in cells. MRPL4 interacts with other ribosomal proteins such as MRPL3 and MRPL12 facilitating the coordination of protein synthesis within the mitochondrion. This process influences cellular respiration and bioenergetics which are critical for adapting to energy requirements.

Associated diseases and disorders

MRPL4 is associated with conditions like mitochondrial disorders and cardiac diseases. Alterations in MRPL4 expression or function can disrupt mitochondrial protein synthesis leading to impaired oxidative phosphorylation and energy production. Such mitochondrial dysfunction is linked to disorders like mitochondrial encephalomyopathy and cardiomyopathy. MRPL4's interactions with other ribosomal proteins ensure that changes in its structure or expression could influence disease progression making it a target for further research in mitochondrial medicine.