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Literature summary for 2.7.8.17 extracted from

  • Franke, M.; Braulke, T.; Storch, S.
    Transport of the GlcNAc-1-phosphotransferase alpha/beta-subunit precursor protein to the golgi apparatus requires a combinatorial sorting motif (2013), J. Biol. Chem., 288, 1238-1249.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli, COS-7 cells and HeLa cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
K1236A/R1237A/K1238A mutant containing a mutation of C-terminal endoplasmic reticulum export motif mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker Homo sapiens
K1236M proteolytic cleavage of mutant is not affected. Mutant is localised mainly in the Golgi apparatus Homo sapiens
K4Q patient mutation K4Q impairs the endoplasmic reticulum export of the PT alpha/beta-subunit precursor protein. Mutant shows reduced levels of the PT beta-subunit. Mutant is localised in the Golgi apparatus and in the endoplasmic reticulum Homo sapiens
L5A/L6A replacement of the N-terminal dileucine motif with alanine residues results in a significant reduction of the PT alpha/beta-subunit precursor protein cleavage. Densitometric evaluation of intensities of immunoreactive bands show that the formation of the beta-subunit is reduced by 46% compared with the wild-type construct. Mutant mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker Homo sapiens
L5A/L6A/R1253A/I1254A/R1255A double mutant containing a mutation of N-terminal and C-terminal endoplasmic reticulum export motif shows a strong inhibitory effect on cleavage of the PT alpha/beta-subunit precursor protein. Mutation leads to retention in the endoplasmic reticulum Homo sapiens
L5A/L6A/R1253L/I1254L/R1255X the transfer of the dileucine motif to the C-terminal domain replacing the dibasic-based motif 1253RIR1255 in combination with the substitution of the N-terminal dileucine motif, blocks the endoplasmic exit and the subsequent proteolytic cleavage to mature PT beta-subunit Homo sapiens
L5R/L6R/R1253A/I1254A/R1255A substitution of the N-terminal L-Leu/L-Leu motif by dibasic-based motifs RIR or RR in combination with alanine substitution of the C-terminal motif prevents the alpha/beta-subunit precursor protein from reaching the Golgi apparatus for cleavage Homo sapiens
R1242A/R1243A/R1244A by mutation of the arginine motif in beta subunit it is shown that this signal is not a functional endoplasmic reticulum retention signal Homo sapiens
R1244A/R1245A/R1246A mutant containing a mutation of C-terminal endoplasmic reticulum export motif mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker Homo sapiens
R1253A/I1254A/R1255A mutant containing a mutation of C-terminal endoplasmic reticulum export motif mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker Homo sapiens
R925A mutation results in an uncleavable PT alpha/beta-subunit precursor protein. Mutant co-localizes mainly with the cis-Golgi marker protein, no detection in endoplasmic reticulum Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum PT alpha/beta-subunit precursor protein is exported into the Golgi apparatus whereas coexpressed separate alpha- and beta-subunits fail to reach the cis-Golgi compartment. Endoplasmic reticulum exit of the PT alpha/beta-subunit precursor protein is dependent on Sar-1 protein Homo sapiens 5783
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Golgi apparatus uncleaved and cleaved forms of the PT alpha/beta-subunit precursor are localized in the Golgi apparatus Homo sapiens 5794
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q3T906
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Synonyms

Synonyms Comment Organism
N-acetylglucosamine-1-phosphotransferase
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Homo sapiens
PT alpha/beta subunit precursor protein
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Homo sapiens