Anti-FBXL22 antibody

Supplementary info

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

Activity summary

FBXL22 also known as F-box and leucine-rich repeat protein 22 is a part of the F-box protein family characterized by an F-box motif. This protein weighs approximately 47 kDa. It is a component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which is involved in tagging proteins for degradation by the proteasome. FBXL22 exhibits expression in various tissues with higher levels observed in the testis and brain. It serves as a substrate recognition component targeting specific proteins for ubiquitination facilitating protein turnover and regulation.

Biological function summary

The role of FBXL22 spans beyond proteasomal degradation. It participates in regulating cell cycle progression and DNA damage response impacting cellular homeostasis. As a part of the SCF complex FBXL22 interacts with SKP1 and CUL1 to form a functional E3 ligase which is important in maintaining protein quality control. This function helps in eliminating misfolded or damaged proteins ensuring cellular integrity and defense against stress conditions.

Pathways

FBXL22 acts within the context of the ubiquitin-proteasome system. It plays a role in pathways such as protein quality control and DNA repair. In these pathways FBXL22 associates with proteins like TP53 and MDM2 influencing cellular responses to DNA damage and stress. Its activity impacts the balance between cell survival and apoptosis positioning it as a modulator within cellular stress response pathways.

Associated diseases and disorders

FBXL22 has implications in cancer and neurodegenerative diseases. Aberrant expression or mutations in FBXL22 can lead to unregulated protein degradation contributing to tumorigenesis. In cancer FBXL22 might interact with proteins such as p53 affecting its stability and function therefore impacting cell cycle checkpoints. Moreover in neurodegenerative conditions altered FBXL22 activity may contribute to the accumulation of damaged proteins exacerbating disease progression.