网格蛋白
生物
网格蛋白接合器蛋白
拟南芥
细胞生物学
高尔基体
内吞循环
内化
内吞作用
内体
信号转导衔接蛋白
蛋白质组
拟南芥
分泌途径
生物化学
受体
信号转导
基因
内质网
细胞内
突变体
作者
Dana A Dahhan,Gregory D Reynolds,Jessica J Cárdenas,Dominique Eeckhout,Alexander Johnson,Klaas Yperman,Walter A Kaufmann,Nou Vang,Xu Yan,Inhwan Hwang,Antje Heese,Geert De Jaeger,Jiri Friml,Daniel Van Damme,Jianwei Pan,Sebastian Y Bednarek
出处
期刊:The Plant Cell
[Oxford University Press]
日期:2022-01-01
卷期号:34 (6): 2150-2173
被引量:13
标识
DOI:10.1093/plcell/koac071
摘要
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 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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