Disease relevance of GNPTG

• Missense mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTA) in a patient with mucolipidosis II induces changes in the size and cellular distribution of GNPTG [1].

High impact information on GNPTG

• The alpha/beta subunits encoded by the GNPTA gene is the catalytic subunit of the enzyme while the gamma recognition subunit is encoded by the GNPTAG gene [2].
• A different electrophoretic mobility of the 97 kDa GNPTG dimer suggested posttranslational modification abrogating the compartmentalization of GNPTG in the Golgi apparatus [1].
• The data indicate that defects in genes other than GNPTAG can be linked to ML III contributing to the variability of the phenotype [3].
• Genomic organisation of the UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTAG) and its mutations in mucolipidosis III [4].
• A novel mutation in UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTAG) in two siblings with mucolipidosis type III alters a used glycosylation site [5].

Anatomical context of GNPTG

• Western blot analysis of extracts from control fibroblasts detect a 97 kDa glycosylated dimer whereas ML III cells contain a GNPTAG dimer of reduced molecular mass [5].

Associations of GNPTG with chemical compounds

• These data suggest that the loss of the used glycosylation site in the gamma subunit may affect the intracellular localization of GNPTAG and the overall efficiency of M6P formation [5].

Other interactions of GNPTG

• The data demonstrate that defective GNPTA not only impairs lysosomal enzyme targeting but also the availability of intact GNPTG required for phosphotransferase activity and assembly of subunits [1].

References