MSL complex subunit 3 (MSL3)

MSL complex subunit 3 (MSL3) is a nuclear protein and an essential, non-catalytic component of the MSL (male-specific lethal) complex, which plays a vital role in chromatin remodeling and transcriptional regulation, particularly in X chromosome dosage compensation. MSL3 contains a chromodomain and an MRG domain, enabling it to interact with both nucleic acids and other proteins within the complex. It helps mediate the acetylation of histone H4 at lysine 16 (H4K16ac), an epigenetic mark that leads to chromatin decompaction and increased transcriptional activity, particularly for genes on the X chromosome. MSL3 executes its function primarily by binding methylated histone H4 at Lys-20 (H4K20Me1) in a DNA-dependent manner and is thought to be involved in X inactivation and maintenance of genome integrity. Genetic defects in MSL3 are linked to rare developmental syndromes and possibly autism spectrum disorders, indicating its crucial role in normal development and gene expression[1][2][3][4]. No known approved drugs directly target MSL3, and it is not currently considered a direct therapeutic target; instead, it functions as a component of a chromatin-modifying complex essential for epigenetic regulation[3].

Other names

MSL3L1MSL3-like 1Male-specific lethal 3 homologMale-specific lethal-3 homolog 1Male-specific lethal-3 protein-like 1MRSXBAMRXS36MRXSBA

Not applicable; no known therapeutic drugs specifically target MSL3