Phosphoglucomutase-like protein 5 (PGM5)

Phosphoglucomutase-like protein 5 (PGM5), also referred to as aciculin, is a protein found primarily in muscle tissue where it functions as a dynamic structural multi-adaptor involved in myofibril organization and maintenance[2]. PGM5 interacts with key muscle proteins such as Filamin C (FLNc) and Xin actin-binding proteins, localizing to critical muscle cell structures including intercalated discs, myotendinous junctions, and Z-discs[2]. Unlike its close homolog phosphoglucomutase 1 (PGM1), PGM5 does not exhibit enzymatic activity for phosphoglucomutase reactions, likely due to differences in active-site loops, but retains high structural similarity within the alpha-D-phosphohexomutase family[1]. Functional studies demonstrate that PGM5 is crucial for muscle development and remodeling, with loss-of-function experiments leading to severe myofibril defects in cell and animal models[2]. Currently, PGM5 is not recognized as a therapeutic target, and there are no known drugs targeting this protein[1][2][4].

Other names

aciculinPGMRPPGM5_HUMAN