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- aggregation classification "A1".
- aggregation creator B437935.
- aggregation creator B437936.
- aggregation creator B437937.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1995985.bibtex.
- aggregation hasFormat 1995985.csv.
- aggregation hasFormat 1995985.dc.
- aggregation hasFormat 1995985.didl.
- aggregation hasFormat 1995985.doc.
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- aggregation hasFormat 1995985.txt.
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- aggregation hasFormat 1995985.yaml.
- aggregation isPartOf urn:issn:1001-0602.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "The AP-3 adaptor complex is required for vacuolar function in Arabidopsis".
- aggregation abstract "Subcellular trafficking is required for a multitude of functions in eukaryotic cells. It involves regulation of cargo sorting, vesicle formation, trafficking and fusion processes at multiple levels. Adaptor protein (AP) complexes are key regulators of cargo sorting into vesicles in yeast and mammals but their existence and function in plants have not been demonstrated. Here we report the identification of the protein-affected trafficking 4 (pat4) mutant defective in the putative delta subunit of the AP-3 complex. pat4 and pat2, a mutant isolated from the same GFP imaging-based forward genetic screen that lacks a functional putative AP-3 beta, as well as dominant negative AP-3 mu transgenic lines display undistinguishable phenotypes characterized by largely normal morphology and development, but strong intracellular accumulation of membrane proteins in aberrant vacuolar structures. All mutants are defective in morphology and function of lytic and protein storage vacuoles (PSVs) but show normal sorting of reserve proteins to PSVs. Immunoprecipitation experiments and genetic studies revealed tight functional and physical associations of putative AP-3 beta and AP-3 delta subunits. Furthermore, both proteins are closely linked with putative AP-3 mu and sigma subunits and several components of the clathrin and dynamin machineries. Taken together, these results demonstrate that AP complexes, similar to those in other eukaryotes, exist in plants, and that AP-3 plays a specific role in the regulation of biogenesis and function of vacuoles in plant cells.".
- aggregation authorList BK763917.
- aggregation endPage "1722".
- aggregation issue "12".
- aggregation startPage "1711".
- aggregation volume "21".
- aggregation aggregates 1996000.
- aggregation isDescribedBy 1995985.
- aggregation similarTo cr.2011.99.
- aggregation similarTo LU-1995985.