Structural highlights
Disease
[GNPTA_HUMAN] Mucolipidosis type 2;Mucolipidosis type 3. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Defects in GNPTAB have been suggested to play a role in susceptibility to persistent stuttering. Stuttering is a common speech disorder characterized by repetitions, prolongations, and interruptions in the flow of speech.[1]
Function
[GNPTA_HUMAN] Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment.[2] [3]
References
- ↑ Kang C, Riazuddin S, Mundorff J, Krasnewich D, Friedman P, Mullikin JC, Drayna D. Mutations in the lysosomal enzyme-targeting pathway and persistent stuttering. N Engl J Med. 2010 Feb 25;362(8):677-85. doi: 10.1056/NEJMoa0902630. Epub 2010, Feb 10. PMID:20147709 doi:http://dx.doi.org/10.1056/NEJMoa0902630
- ↑ Qian Y, Lee I, Lee WS, Qian M, Kudo M, Canfield WM, Lobel P, Kornfeld S. Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase. J Biol Chem. 2010 Jan 29;285(5):3360-70. doi: 10.1074/jbc.M109.068650. Epub 2009 , Dec 2. PMID:19955174 doi:http://dx.doi.org/10.1074/jbc.M109.068650
- ↑ Qian Y, Flanagan-Steet H, van Meel E, Steet R, Kornfeld SA. The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition module. Proc Natl Acad Sci U S A. 2013 Jun 18;110(25):10246-51. doi:, 10.1073/pnas.1308453110. Epub 2013 Jun 3. PMID:23733939 doi:http://dx.doi.org/10.1073/pnas.1308453110
