Anti-RRBP1 antibody

Supplementary info

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

Activity summary

RRBP1 also known as ribosome binding protein 1 is a significant endoplasmic reticulum (ER) membrane protein involved in ribosome binding and translocation of newly synthesized proteins. This protein also goes by the name p180 and has a molecular mass of approximately 180 kDa. RRBP1 is predominantly expressed in cells with high secretory activity such as those in the pancreas and liver where it assists in the robust production and processing of proteins required for secretion.

Biological function summary

RRBP1 facilitates the initial binding of ribosomes to the ER membrane a process essential for the proper targeting and translocation of proteins entering the secretory pathway. This protein is integral to the ribosome-ER association acting as a scaffold that stabilizes ribosome attachment during translation. RRBP1 functions as part of a larger translocon complex that includes proteins such as Sec61 which together form a channel for translocating polypeptides into the ER lumen or integrating them into the ER membrane.

Pathways

The protein is essential in protein synthesis and secretion pathways. RRBP1 coordinates with signal recognition particle-dependent pathways where it partners with proteins like Sec61 to ensure accurate translocation of secretory and membrane proteins across the ER membrane. In the unfolded protein response (UPR) pathway RRBP1 might also interact with ER chaperones to assist in protein folding and maintain cellular homeostasis under stress conditions.

Associated diseases and disorders

Abnormalities in RRBP1 expression and function have associations with certain types of cancer including breast cancer where its overexpression contributes to tumor progression. Additionally RRBP1 dysregulation may relate to neurodegenerative diseases through its role in protein folding and ER stress response. Proteins like BiP (Grp78) an important chaperone involved in UPR may link to RRBP1 in these pathological states highlighting potential intersections between ER stress and disease pathways.