Journal
PLANT CELL
Volume 25, Issue 8, Pages 2958-2969Publisher
AMER SOC PLANT BIOLOGISTS
DOI: 10.1105/tpc.113.114082
Keywords
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Funding
- Japan Society for the Promotion of Science [22000014, 25120715, 25840108, 25650096]
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The adaptor protein-2 (AP-2) complex is a heterotetramer involved in clathrin-mediated endocytosis of cargo proteins from the plasma membrane in animal cells. The homologous genes of AP-2 subunits are present in the genomes of plants; however, their identities and roles in endocytic pathways are not clearly defined in plants. Here, we reveal the molecular composition of the AP-2 complex of Arabidopsis thaliana and its dynamics on the plasma membrane. We identified all of the alpha-, beta-, sigma-, and mu-subunits of the AP-2 complex and detected a weak interaction of the AP-2 complex with clathrin heavy chain. The mu-subunit protein fused to green fluorescent protein (AP2M-GFP) was localized to the plasma membrane and to the cytoplasm. Live-cell imaging using a variable-angle epifluorescence microscope revealed that AP2M-GFP transiently forms punctate structures on the plasma membrane. Homozygous ap2m mutant plants exhibited abnormal floral structures, including reduced stamen elongation and delayed anther dehiscence, which led to a failure of pollination and a subsequent reduction of fertility. Our study provides a molecular basis for understanding AP-2-dependent endocytic pathways in plants and their roles in floral organ development and plant reproduction.
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