Abstract
Cytokinesis is the process of partitioning the cytoplasm of a dividing cell, thereby completing mitosis. Cytokinesis in the plant cell is achieved by the formation of a new cell wall between daughter nuclei using components carried in Golgi-derived vesicles that accumulate at the midplane of the phragmoplast and fuse to form the cell plate. Proteins that play major roles in the development of the cell plate in plant cells are not well defined. Here, we report that an AP180 amino-terminal homology/epsin amino-terminal homology domain-containing protein from Arabidopsis (Arabidopsis thaliana) is involved in clathrin-coated vesicle formation from the cell plate. Arabidopsis Epsin-like Clathrin Adaptor1 (AtECA1; At2g01600) and its homologous proteins AtECA2 and AtECA4 localize to the growing cell plate in cells undergoing cytokinesis and also to the plasma membrane and endosomes in nondividing cells. AtECA1 (At2g01600) does not localize to nascent cell plates but localizes at higher levels to expanding cell plates even after the cell plate fuses with the parental plasma membrane. The temporal and spatial localization patterns of AtECA1 overlap most closely with those of the clathrin light chain. In vitro protein interaction assays revealed that AtECA1 binds to the clathrin H chain via its carboxyl-terminal domain. These results suggest that these AP180 amino-terminal homology/epsin amino-terminal homology domain-containing proteins, AtECA1, AtECA2, and AtECA4, may function as adaptors of clathrin-coated vesicles budding from the cell plate.
Highlights
Cytokinesis is the process of partitioning the cytoplasm of a dividing cell, thereby completing mitosis
The sGFP fusion constructs AtECA1:sGFP, AtECA2:sGFP, and AtECA4:sGFP were transformed into protoplasts from leaf tissues of Arabidopsis using polyethylene glycol-mediated transformation
Three A/epsin N-terminal homology (ENTH) domain proteins, AtECA1, AtECA2, and AtECA4, which are characterized in this study, are most distantly related to the two A/ENTH domaincontaining proteins AtEpsinR1 and AtEpsinR2, which were characterized previously in plant cells (Song et al, 2006; Lee et al, 2007)
Summary
Cytokinesis is the process of partitioning the cytoplasm of a dividing cell, thereby completing mitosis. In vitro protein interaction assays revealed that AtECA1 binds to the clathrin H chain via its carboxyl-terminal domain These results suggest that these AP180 amino-terminal homology/epsin amino-terminal homology domain-containing proteins, AtECA1, AtECA2, and AtECA4, may function as adaptors of clathrin-coated vesicles budding from the cell plate. Recent studies have revealed that many vesicle trafficking-related proteins are involved in cell plate formation These proteins include the cytokinesis-specific t-SNARE KNOLLE (Lauber et al, 1997), a syntaxin-binding protein, KEULE (Assaad et al, 2001), AtSNAP33 (Heese et al, 2001), dynaminrelated proteins (DRPs; Hong et al, 2003; Ito et al, 2012), ESCRT (for endosomal sorting complex required for transport) components, and proteins of the exocyst complex (Fendrych et al, 2010). The results provide evidence that several A/ENTH domain-containing proteins, including At2g01600, localize to the growing cell plate and suggest that the proteins may serve as adaptors for clathrin in CCV-mediated endocytosis at the growing cell plate
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