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  • 1
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    A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-07-02
    Description: Mucolipidosis II is a severe lysosomal storage disorder caused by defects in the alpha and beta subunits of the hexameric N-acetylglucosamine-1-phosphotransferase complex essential for the formation of the mannose 6-phosphate targeting signal on lysosomal enzymes. Cleavage of the membrane-bound alpha/beta-subunit precursor by an unknown protease is required for catalytic activity. Here we found that the alpha/beta-subunit precursor is cleaved by the site-1 protease (S1P) that activates sterol regulatory element-binding proteins in response to cholesterol deprivation. S1P-deficient cells failed to activate the alpha/beta-subunit precursor and exhibited a mucolipidosis II-like phenotype. Thus, S1P functions in the biogenesis of lysosomes, and lipid-independent phenotypes of S1P deficiency may be caused by lysosomal dysfunction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marschner, Katrin -- Kollmann, Katrin -- Schweizer, Michaela -- Braulke, Thomas -- Pohl, Sandra -- New York, N.Y. -- Science. 2011 Jul 1;333(6038):87-90. doi: 10.1126/science.1205677.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21719679" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Cell Line ; Cholesterol/*metabolism ; Chondrocytes/cytology ; Cricetinae ; Cricetulus ; Enzyme Precursors/chemistry/*metabolism ; HeLa Cells ; Humans ; Lipid Metabolism ; Lysosomes/enzymology/*metabolism/ultrastructure ; Mannosephosphates/metabolism ; Mice ; Morphogenesis ; Mucolipidoses/enzymology/genetics/metabolism/pathology ; N-Acetylgalactosamine-4-Sulfatase/metabolism ; Osteogenesis ; Proprotein Convertases/genetics/*metabolism ; Protein Subunits/chemistry/metabolism ; RNA, Small Interfering ; Serine Endopeptidases/genetics/*metabolism ; Transferases (Other Substituted Phosphate Groups)/chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Subunit interactions of the disease-related hexameric GlcNAc-1-phosphotransferase complex (2015)
    Oxford University Press
    Details
    Publication Date: 2015-11-06
    Description: The multimeric GlcNAc-1-phosphotransferase complex catalyzes the formation of mannose 6-phosphate recognition marker on lysosomal enzymes required for receptor-mediated targeting to lysosomes. GNPTAB and GNPTG encode the α/β-subunit precursor membrane proteins and the soluble -subunits, respectively. Performing extensive mutational analysis, we identified the binding regions of -subunits in a previously uncharacterized domain of α-subunits comprising residues 535–698, named GNPTG binding (GB) domain. Both the deletion of GB preventing -subunit binding and targeted deletion of GNPTG led to significant reduction in GlcNAc-1-phosphotransferase activity. We also identified cysteine 70 in α-subunits to be involved in covalent homodimerization of α-subunits which is, however, required neither for interaction with -subunits nor for catalytic activity of the enzyme complex. Finally, binding assays using various -subunit mutants revealed that residues 130–238 interact with glycosylated α-subunits suggesting a role for the mannose 6-phosphate receptor homology domain in α-subunit binding. These studies provide new insight into the assembly of the GlcNAc-1-phosphotransferase complex, and the functions of distinct domains of the α- and -subunits.
    Print ISSN: 0964-6906
    Electronic ISSN: 1460-2083
    Topics: Biology , Medicine
    Published by Oxford University Press
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