N-acetylglucosamine phosphotransferase
From Proteopedia
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Post-translational modifications such as interchain and intramolecular disulfide bonds may occur via GlcNAc-phosphotransferase in the cytoplasm outside of the nucleus, including the protein glycosylation on serine and threonine residues. Any imbalance of phosphorylation can lead to diseases including cancer, diabetes, and neurodegenerative diseases <ref>European Bioinformatics Institute. Protein Information Resource. SIB Swiss Institute of Bioinformatics.</ref>. Management of phosphorylation and other modifications performed by GlcNAc-phosphotransferase can allow for better diagnoses and treatments of such diseases. | Post-translational modifications such as interchain and intramolecular disulfide bonds may occur via GlcNAc-phosphotransferase in the cytoplasm outside of the nucleus, including the protein glycosylation on serine and threonine residues. Any imbalance of phosphorylation can lead to diseases including cancer, diabetes, and neurodegenerative diseases <ref>European Bioinformatics Institute. Protein Information Resource. SIB Swiss Institute of Bioinformatics.</ref>. Management of phosphorylation and other modifications performed by GlcNAc-phosphotransferase can allow for better diagnoses and treatments of such diseases. | ||
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Revision as of 03:58, 15 April 2019
N-acetylglucosamine (GlcNAc) phosphotransferase is a cis-Golgi-localized enzyme that recognizes the specific protein sequence in newly synthesized lysosomal enzymes and transfers phosphorylated GlcNAc groups [1],[2]. This enzyme is hexameric, composed of two alpha, two beta, and two gamma subunits [3].
Disease
Mucolipidosis II is an autosomal recessive hereditary phenotypic disease caused by disruptions of the alpha and beta subunits. This disease presents symptoms of mental retardation and skeletal changes as acid mucopolysaccharides, sphingolipids, and/or glycolipids concentrate in visceral and mesenchymal cells in neural tissue [4],[5]. In a study by Kudo et al, patients with the disease had either absent or reduced alpha/beta transcription; however, all patients had normal gamma subunit levels [6]. This suggests that the alpha and/or the beta subunit contains enzymatic qualities.
Post-translational modifications such as interchain and intramolecular disulfide bonds may occur via GlcNAc-phosphotransferase in the cytoplasm outside of the nucleus, including the protein glycosylation on serine and threonine residues. Any imbalance of phosphorylation can lead to diseases including cancer, diabetes, and neurodegenerative diseases [7]. Management of phosphorylation and other modifications performed by GlcNAc-phosphotransferase can allow for better diagnoses and treatments of such diseases.
Structural highlights
The alpha and beta subunits result from a single cDNA and formed by proteolysis at a lysine-aspartate bond on the alpha/beta precursor [8]. The alpha and beta subunits are encoded by the GNPTAB gene, but the gamma subunit is encoded independently by the GNPTG gene, making GlcNAc an exception to the Garrod-Beadle principle that one enzyme is encoded by one gene [9],[10].
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