Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components
SCIE
SCOPUS
- Title
- Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components
- Authors
- Dahhan, Dana A; Reynolds, Gregory D; Cárdenas, Jessica J; Eeckhout, Dominique; Johnson, Alexander; Yperman, Klaas; Kaufmann, Walter A; Vang, Nou; Yan, Xu; Hwang, Inhwan; Heese, Antje; De Jaeger, Geert; Friml, Jiri; Van Damme, Daniel; Pan, Jianwei; Bednarek, Sebastian Y
- Date Issued
- 2022-03
- Publisher
- American Society of Plant Biologists
- Abstract
- In eukaryotes, clathrin-coated vesicles (CCVs) facilitate the internalization of material from the cell surface as well as the movement of cargo in post-Golgi trafficking pathways. This diversity of functions is partially provided by multiple monomeric and multimeric clathrin adaptor complexes that provide compartment and cargo selectivity. The adaptor-protein AP-1 complex operates as part of the secretory pathway at the trans-Golgi network, while the AP-2 complex and the TPLATE complex (TPC) jointly operate at the plasma membrane to execute clathrin-mediated endocytosis. Key to our further understanding of clathrin-mediated trafficking in plants will be the comprehensive identification and characterization of the network of evolutionarily conserved and plant-specific core and accessory machinery involved in the formation and targeting of CCVs. To facilitate these studies, we have analyzed the proteome of enriched trans-Golgi network/early endosome-derived and endocytic CCVs isolated from dividing and expanding suspension-cultured Arabidopsis (Arabidopsis thaliana) cells. Tandem mass spectrometry analysis results were validated by differential chemical labeling experiments to identify proteins co-enriching with CCVs. Proteins enriched in CCVs included previously characterized CCV components and cargos such as the vacuolar sorting receptors in addition to conserved and plant-specific components whose function in clathrin-mediated trafficking has not been previously defined. Notably, in addition to AP-1 and AP-2, all subunits of the AP-4 complex, but not AP-3 or AP-5, were found to be in high abundance in the CCV proteome. The association of AP-4 with suspension-cultured Arabidopsis CCVs is further supported via additional biochemical data.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/110304
- DOI
- 10.1093/plcell/koac071
- ISSN
- 1040-4651
- Article Type
- Article
- Citation
- Plant Cell, vol. 34, no. 6, page. 1 - 48, 2022-03
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