Anti-TIMM17B antibody

Supplementary info

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

Activity summary

TIMM17B also known as Translocase of Inner Mitochondrial Membrane 17 homolog B is a protein component with a molecular mass of approximately 21 kDa. TIMM17B is importantly involved in the translocation of proteins across the mitochondrial inner membrane. This protein is expressed in various tissues but shows higher expression in testis and heart. TIMM17B plays a critical role in mitochondrial function by acting as a channel-forming protein within the TIMM complex.

Biological function summary

TIMM17B integrates its function into the import machinery for mitochondrial proteins. It is part of the TIM22 complex an important multi-protein system that mediates the insertion and assembly of certain hydrophobic proteins into the mitochondrial inner membrane. TIMM17B works in coordination with other TIMM proteins such as TIM22 to facilitate the transfer and integration of mitochondrial carrier proteins. This integration supports the effective maintenance of mitochondrial functions which are essential for cellular energy metabolism.

Pathways

TIMM17B plays a significant role in the mitochondrial protein import pathway. This process involves the transport of proteins synthesized in the cytosol into the mitochondria which is essential for mitochondrial biogenesis and function. TIMM17B is also linked with the oxidative phosphorylation pathway through its involvement in maintaining mitochondrial membrane potential. Proteins like TIMM23 and TIMM50 are closely related to TIMM17B within these pathways providing important support for its function in importing proteins necessary for energy production.

Associated diseases and disorders

TIMM17B has been connected to mitochondrial disorders and neurodegenerative diseases. Disturbances in its function or expression can affect mitochondrial integrity contributing to conditions such as Leigh syndrome. Moreover TIMM17B shows associations with Alzheimer's disease where defects in mitochondrial dynamics and energy metabolism play a role. These connections also involve the protein PINK1 which is associated with autosomal recessive early-onset Parkinson's disease highlighting the importance of mitochondrial quality control in neurodegenerative disorders.