Recombinant Human FKBP23 protein (Fc Chimera)

Supplementary information

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

FKBP23 also known as FK506-binding protein 23 is a member of the FKBP family of proteins which serve as peptidyl-prolyl cis-trans isomerases. This protein has a molecular mass of approximately 23 kDa. FKBP23 localizes primarily in the endoplasmic reticulum (ER) where it associates with calcium-binding environments. It is expressed in various tissues but exhibits higher levels in the brain and heart indicating its specialized roles in these organs.

Biological function summary

FKBP23 functions as a chaperone assisting in the proper folding of nascent proteins within the endoplasmic reticulum. It's known to partake in protein folding processes working in conjunction with other molecular chaperones to secure protein homeostasis. FKBP23 forms part of complexes that stabilize newly synthesized proteins until they reach their functional conformation highlighting its role in maintaining cellular proteostasis.

Pathways

FKBP23 is involved in the unfolded protein response (UPR) pathway and calcium signaling processes. In the UPR pathway FKBP23 assists in mitigating stress in the ER caused by the accumulation of misfolded proteins. It also interacts with other proteins like BiP/Grp78 an ER chaperone integral to stress response mediation. This protein impacts calcium signaling by modulating calcium retention within the ER influencing pathways critical for cell survival and apoptosis.

FKBP23 has been linked to neurodegenerative diseases and cardiac dysfunction. It plays a role in diseases such as Parkinson's where protein misfolding and ER stress significantly contribute to pathogenesis. FKBP23 interacts with proteins linked to these disorders such as alpha-synuclein involved in protein aggregation processes. Additionally altered FKBP23 activity is associated with cardiac hypertrophy where its impact on calcium regulation affects cardiac muscle function implicating it in related pathologies through modulation of calcium-dependent signaling.