期刊
PLANT CELL
卷 34, 期 6, 页码 2150-2173出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/plcell/koac071
关键词
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资金
- National Science Foundation [1121998, 1614915]
- Vilas Associate Award (University of Wisconsin, Madison, Graduate School)
- National Natural Science Foundation of China [91754104, 31820103008, 31670283]
- National Research Foundation of Korea [2019R1A2B5B03099982]
- Scientific Service Units (SSU) of Institute of Science and Technology Austria
- Austrian Science Fund (FWF) [I3630B25]
- National Science Foundation (NSF IOS) [1147032, 1758843]
- European Research Council [682436]
- European Research Council (ERC) [682436] Funding Source: European Research Council (ERC)
- National Research Foundation of Korea [4120200313623] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [1758843, 1147032] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1614915] Funding Source: National Science Foundation
In this study, mass spectrometry was used to analyze the proteome of Arabidopsis suspension-cultured cell clathrin-coated vesicles (CCVs). The study identified evolutionarily conserved and plant-specific factors associated with CCVs. Notably, the AP-4 complex was found to be abundantly present in the CCV proteome.
Mass spectrometry analyses of Arabidopsis suspension-cultured cell clathrin-coated vesicles delineate the plant clathrin-coated vesicle (CCV) proteome and identify evolutionarily conserved and plant-specific CCV-associated factors. 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 assembly polypeptide-1 (AP-1) complex operates as part of the secretory pathway at the trans-Golgi network (TGN), while the AP-2 complex and the TPLATE complex 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 TGN/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.
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