Alpha-crystallin B chain (CRYAB)

Alpha-crystallin B chain is a small heat shock protein encoded by the CRYAB gene in humans. It serves as a molecular chaperone that binds misfolded proteins to prevent their aggregation, protects cells from stress-induced apoptosis, and maintains the architecture of muscle and lens cells. This protein is abundant in the eye lens, where its stability is crucial for lens transparency, but it also exists in many tissues including muscle, heart, and brain. Mutations in CRYAB are associated with inherited cardiac and skeletal muscle myopathies, cataract, cancers, and neurodegenerative diseases. Alpha-crystallin B chain operates as part of large, heterogeneous complexes, and its activity can be modulated by post-translational modifications[1][3][5][8].

Other names

HspB5Heat shock protein beta-5αB-crystallinAlpha-B crystallin

Not a direct drug target; however, in preclinical models, modulation of chaperone function or expression can alter protein aggregation in disease contexts