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Description

Phosphoglucomutase-like protein 5 (UniProt: Q15124, also known as Aciculin, Phosphoglucomutase-related protein, PGM-RP) is encoded by the PGM5 (also known as PGMRP) gene (Gene ID: 5239) in human. Aciculin is a dystrophin and utrophin-binding protein that is highly homologous to the glycolytic enzyme phosphoglucomutase type 1. However, it lacks phosphoglucomutase activity. Aciculin is a component of adherens-type cell-cell and cell-matrix junctions and is concentrated in focal contacts at the ends of actin bundles and associates with actin filaments. Aciculin is also reported to be an interaction partner of Filamin C and Xin proteins. Higher levels of Aciculin are reported in smooth and cardiac muscle and lower levels are present in skeletal muscle, liver, kidney and brain tissue. In striated muscle, it mainly localizes to the intercalated discs of the heart and to myotendinous junctions. Low levels of Aciculin are expressed in 10-12-week-old fetus and these levels increase progressively into infancy reaching maximum levels at maturity. Two isoforms of Aciculin have been reported that are produced by alternative splicing. Aciculin knockdown in myotubes is shown to cause failure in myofibril assembly, alignment and membrane attachment, and a massive reduction in myofibril number. (Ref.: Molt, S., et al., (2014). J. Cell Sci.127(16), 3578-3592).