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http://purl.uniprot.org/citations/23400704http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23400704http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23400704http://www.w3.org/2000/01/rdf-schema#comment"N-Glycan processing is one of the most important cellular protein modifications in plants and as such is essential for plant development and defense mechanisms. The accuracy of Golgi-located processing steps is governed by the strict intra-Golgi localization of sequentially acting glycosidases and glycosyltransferases. Their differential distribution goes hand in hand with the compartmentalization of the Golgi stack into cis-, medial-, and trans-cisternae, which separate early from late processing steps. The mechanisms that direct differential enzyme concentration are still unknown, but the formation of multienzyme complexes is considered a feasible Golgi protein localization strategy. In this study, we used two-photon excitation-Förster resonance energy transfer-fluorescence lifetime imaging microscopy to determine the interaction of N-glycan processing enzymes with differential intra-Golgi locations. Following the coexpression of fluorescent protein-tagged amino-terminal Golgi-targeting sequences (cytoplasmic-transmembrane-stem [CTS] region) of enzyme pairs in leaves of tobacco (Nicotiana spp.), we observed that all tested cis- and medial-Golgi enzymes, namely Arabidopsis (Arabidopsis thaliana) Golgi α-mannosidase I, Nicotiana tabacum β1,2-N-acetylglucosaminyltransferase I, Arabidopsis Golgi α-mannosidase II (GMII), and Arabidopsis β1,2-xylosyltransferase, form homodimers and heterodimers, whereas among the late-acting enzymes Arabidopsis β1,3-galactosyltransferase1 (GALT1), Arabidopsis α1,4-fucosyltransferase, and Rattus norvegicus α2,6-sialyltransferase (a nonplant Golgi marker), only GALT1 and medial-Golgi GMII were found to form a heterodimer. Furthermore, the efficiency of energy transfer indicating the formation of interactions decreased considerably in a cis-to-trans fashion. The comparative fluorescence lifetime imaging of several full-length cis- and medial-Golgi enzymes and their respective catalytic domain-deleted CTS clones further suggested that the formation of protein-protein interactions can occur through their amino-terminal CTS region."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.org/dc/terms/identifier"doi:10.1104/pp.112.210757"xsd:string
http://purl.uniprot.org/citations/23400704http://purl.org/dc/terms/identifier"doi:10.1104/pp.112.210757"xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Schoberer J."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Schoberer J."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Strasser R."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Strasser R."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Hawes C."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Hawes C."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Liebminger E."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Liebminger E."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Botchway S.W."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/author"Botchway S.W."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/name"Plant Physiol."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/name"Plant Physiol."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/pages"1737-1754"xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/pages"1737-1754"xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/title"Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/title"Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta."xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/volume"161"xsd:string
http://purl.uniprot.org/citations/23400704http://purl.uniprot.org/core/volume"161"xsd:string
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