WD repeat domain 77 (WDR77)

WD repeat domain 77 (WDR77, also known as MEP50 or p44) is an essential WD40-repeat protein that acts as a non-catalytic adaptor and structural cofactor within the methylosome complex, partnering tightly with protein arginine methyltransferase 5 (PRMT5) to mediate the symmetric dimethylation of arginines on histones and spliceosomal Sm proteins[1][3]. This methylation regulates transcription, mRNA splicing, and mRNA stability. WDR77 is a versatile coactivator for steroid hormone receptors, including androgen and estrogen receptors, enhancing hormone-dependent transcription in a manner influenced by its subcellular localization (nuclear or cytoplasmic)[1][2]. It plays a key regulatory role in cell proliferation, cell cycle progression, and differentiation, with its dysregulation linked to tumorigenesis in prostate, breast, ovarian, and lung cancers, as well as gliomas[2][3]. Mutations or aberrant expression of WDR77 disrupt normal chromatin modification and gene expression balance, contributing to oncogenic transformation and progression. There is growing experimental evidence to support WDR77 as a potential biomarker, as well as a therapeutic target for cancer, with modulation of its activity affecting tumor cell proliferation and hormone-responsiveness[1][2][3].

Other names

Methylosome protein WDR77MEP50WD45HKMT1069Nbla10071MEP-50p44Androgen receptor cofactor p44methylosome protein 50testis tissue sperm-binding protein Li 44a

(Experimental) Drugs or compounds suppress WDR77 expression, potentially disrupting PRMT5 methylosome complex activity, influencing cell proliferation and gene expression[1][2]