Document Detail

An A/ENTH domain-containing protein functions as an adaptor for clathrin-coated vesicles on the growing cell plate in Arabidopsis root cells.
MedLine Citation:
PMID:  22635117     Owner:  NLM     Status:  MEDLINE    
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.
Kyungyoung Song; Mihue Jang; Soo Youn Kim; Goeun Lee; Gil-Je Lee; Dae Heon Kim; Yongjik Lee; Wonhwa Cho; Inhwan Hwang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-05-25
Journal Detail:
Title:  Plant physiology     Volume:  159     ISSN:  1532-2548     ISO Abbreviation:  Plant Physiol.     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-07-03     Completed Date:  2012-10-29     Revised Date:  2013-06-24    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1013-25     Citation Subset:  IM    
Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea.
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MeSH Terms
Adaptor Proteins, Signal Transducing / chemistry,  metabolism*
Adaptor Proteins, Vesicular Transport / chemistry,  metabolism*
Arabidopsis / cytology*,  metabolism*
Arabidopsis Proteins / chemistry,  metabolism*
Cell Membrane / metabolism
Clathrin / metabolism
Clathrin-Coated Vesicles / metabolism*
Endosomes / metabolism
Green Fluorescent Proteins / metabolism
Plant Roots / cytology*,  metabolism
Protein Binding
Protein Structure, Tertiary
Protein Transport
Protoplasts / cytology,  metabolism
Recombinant Fusion Proteins / metabolism
Time Factors
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/Adaptor Proteins, Vesicular Transport; 0/Arabidopsis Proteins; 0/Clathrin; 0/ECA1 protein, Arabidopsis; 0/Recombinant Fusion Proteins; 147336-22-9/Green Fluorescent Proteins

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