Molecular chaperone MKKS (MKKS)

Molecular chaperone MKKS is a Group II chaperonin-like protein predominantly localized at the pericentriolar material of centrosomes in human cells[5]. Its primary function is to assist in the proper folding of proteins using ATP hydrolysis and to promote the assembly of the BBSome complex, which is essential for ciliogenesis—the formation and function of primary cilia that mediate important signaling pathways[6][7]. MKKS is critical during early development, particularly in the formation of limbs, heart, and reproductive system, and participates in protein processing and intracellular transport, including the potential movement of key regulatory proteins (e.g., SMARCC1) to the nucleus[2][6]. Pathogenic mutations disrupt its chaperonin activity, cause mislocalization or aggregation at the centrosome, and underlie the genetic syndromes Bardet–Biedl syndrome and McKusick–Kaufman syndrome[1][5][6]. MKKS is not currently considered a direct therapeutic target—no small molecules or biologics are known to modulate its activity clinically[6][7].

Other names

BBS6Bardet-Biedl syndrome 6 proteinMcKusick-Kaufman/Bardet-Biedl syndromes putative chaperoninHMCSKMSMKS