Prohibitin-1 (PHB1) (PHB1)

Prohibitin-1 (PHB1) and Prohibitin-2 (PHB2) form a highly conserved heteromeric complex that functions as a molecular scaffold (UniProt P35232). While primarily known as a mitochondrial chaperone, the prohibitin complex is also localized to the plasma membrane of intestinal epithelial cells (Theiss et al., 2009, PMID: 19136413). In this location, it acts as a receptor for various ligands, including the Vi capsular polysaccharide of Salmonella Typhi, facilitating bacterial entry (Iyengar et al., 2011, PMID: 21903861). The complex is essential for maintaining intestinal homeostasis and mucosal barrier integrity. Clinical studies have shown that PHB1 expression is significantly decreased in the intestinal mucosa of patients with active Inflammatory Bowel Disease (IBD), contributing to mitochondrial dysfunction and oxidative stress (Theiss et al., 2007, PMID: 17468165). Small molecules such as fluorizoline and rocaglates target the prohibitin complex to modulate the Raf-MEK-ERK signaling pathway or induce apoptosis (Moncunill et al., 2015, PMID: 25605861). Consequently, the prohibitin-containing receptor complex represents a dual-purpose target for anti-infective and anti-inflammatory therapies.

Other names

PHB1BAP32ProhibitinPHBProhibitin complex

Binding to the prohibitin complex to disrupt its scaffolding function, thereby inhibiting the Raf-MEK-ERK signaling pathway or inducing BAX-dependent apoptosis.