| First Author | Lee WS | Year | 2007 |
| Journal | J Biol Chem | Volume | 282 |
| Issue | 37 | Pages | 27198-203 |
| PubMed ID | 17652091 | Mgi Jnum | J:124928 |
| Mgi Id | MGI:3722962 | Doi | 10.1074/jbc.M704067200 |
| Citation | Lee WS, et al. (2007) Murine UDP-GlcNAc:Lysosomal Enzyme N-Acetylglucosamine-1-phosphotransferase Lacking the {gamma}-Subunit Retains Substantial Activity toward Acid Hydrolases. J Biol Chem 282(37):27198-203 |
| abstractText | UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase (GlcNAc-1-phosphotransferase) mediates the first step in the synthesis of the mannose 6-phosphate recognition marker on acid hydrolases. The transferase exists as analpha(2)beta(2)gamma(2) hexameric complex with the alpha- and beta-subunits derived from a single precursor molecule. The catalytic function of the transferase is attributed to the alpha- and beta-subunits, whereas the gamma-subunit is believed to be involved in the recognition of a conformation-dependent protein determinant common to acid hydrolases. Using knock-out mice with mutations in either the alpha/beta gene or the gamma gene, we show that disruption of the alpha/beta gene completely abolishes phosphorylation of high mannose oligosaccharides on acid hydrolases whereas knock-out of the gamma gene results in only a partial loss of phosphorylation. These findings demonstrate that the alpha/beta-subunits, in addition to their catalytic function, have some ability to recognize acid hydrolases as specific substrates. This process is enhanced by the gamma-subunit. |
