Mesoderm development LDL receptor chaperone (MESD)

MESD (Mesoderm development LDL receptor chaperone) is a specialized endoplasmic reticulum chaperone that is essential for folding and maturation of low-density lipoprotein receptor (LDLR) family members, particularly the canonical Wnt co-receptors LRP5 and LRP6[1][2][3]. MESD ensures proper formation of the β-propeller/EGF modules in these proteins, enabling their export to the plasma membrane. MESD is critical for embryonic development, as it is essential for mesoderm induction, embryonic polarity, and for postnatal functions including bone formation and neuromuscular junction development[1][3]. The protein contains distinct chaperone and escort domains, allowing it to both template correct receptor folding and escort properly assembled complexes out of the ER[2]. Loss of MESD function causes severe developmental and metabolic defects due to misfolding and ER retention of target LDL receptors, particularly affecting the Wnt/β-catenin signaling axis[1][2][3][4]. No drugs are currently known to target MESD directly. The gene is associated with rare forms of osteogenesis imperfecta and possibly other developmentally-linked diseases[3].

Other names

KIAA0081MESDC2MESDMUNQ1911/PRO4369BOCAMesoderm development candidate 2Mesoderm development proteinRenal carcinoma antigen NY-REN-61OI20LDLR chaperone MESD