Fig. 5: POGLUT1 mutations associated to cause human diseases.
From: Structure, function, and pathology of protein O-glucosyltransferases
Several mutations of POGLUT1 have been implicated in human DDD4/GGD and LGMDR21. So far, only two nonsense mutations are reported in a signal peptide of POGLUT1 in DDD4/GGD patients. Most of the missense, nonsense, and frameshift variants of POGLUT1 are reported in the CAP10 catalytic domain, which harbors many essential amino acids required for O-glucosylation activity. A single change of essential residues of CAP10 domain can abolish O-glucosyltransferase activity as previously observed. The nonsense and frameshift mutations are resulted either in mRNA decay or the formation of a truncated POGLUT1 leading to DDD4/GGD and LGMDR21 disease.
