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RISS 인기검색어
- 검색키워드
- 저자 : 송경영 (검색결과 4 건)
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송경영 포항공과대학교 일반대학원 2012 국내박사
Clathrin is a fundamental coat protein in protein trafficking at the post-Golgi compartments in eukaryotic cells. Because clathrin directly binds neither to membranes nor cargoes, the clathrin-associated proteins called clathrin adaptors in this study are necessary to connect the clathrin with membrane proteins to be transported by clathrin-coated vesicles (CCVs). CCVs are believed to form in the Golgi apparatus and the plasma membrane in plant cells. The genome of Arabidopsis contains genes that encode clathrin and the clathrin adaptor. However, the role of CCVs and how they are formed at the post-Golgi compartments are poorly understood. Few clathrin adaptors have been characterized in plants. In this study, I characterized two different types of clathrin adaptors in Arabidopsis. One is a monomeric A/ENTH domain-containing protein involved in endocytosis at the cell plate in the cells undergoing cytokinesis; the other is a heteroterameric AP1 complex which is involved in protein trafficking from the TGN to either vacuoles or apoplasts. The N-terminal domain of AtECA1 has a unique ANTH domain which can induce tabulation and which interacts with PtdIns(4,5)P2 enriched in the plasma membrane. To characterize the role of AtECA1 and its homologs AtECA2 and AtECA4, I investigated the in vivo localization in planta. AtECA1 localizes to the plasma membrane in non-dividing cells, and to the cell plate in cells undergoing cytokinesis. The excessive amount of proteins and lipid composition are transported to the cell plate via secretory pathway from the Golgi apparatus to build up the cell plate which expands toward the cell wall of the parental cell and then fuses to it. AtECA1 does not localize to the nascent cell plate during late anaphase (the beginning the cytokinesis) but localizes at higher levels to the midplane of the expanding cell plate instead of the growing edge which is accumulated by incoming vesicles derived from the Golgi apparatus. This spatiotemporal localization of AtECA1 overlaps most closely with those of the clathrin light chain. In vitro protein interaction assays revealed that AtECA1 binds to the clathrin heavy chain at its C-terminal domain. These results suggest that these A/ENTH-containing proteins (AtECA1, AtECA2 and AtECA4), may function as adaptors of clathrin-coated vesicles budding from the cell plate. I also investigated the functional characterization of the heteroterameric AP1 complex using genetics, in vivo imaging, and in vivo protein-protein interaction analysises. AtmuB2, one of five gamma-adaptins of Arabidopsis, localizes to the TGN/EE which is the intersection of exocytic and endocytic pathways. The specific interaction between AtmuB2 and gamma-adaptin revealed that AtmuB2 is a component of the AP1 complex, indicating that the function of AtmuB2 represents that of AP-1. Growth retardation and defect in male fertility are observed in atmub2-1 plants and are rescued by the expression of AtmuB2:Myc. Transient trafficking assay of vacuolar and secretory proteins in the protoplast from atmub2-1 and rescued AtmuB2:Myc/atmub2-1 plants reveal that AP-1-dependent CCVs are involved in both vacuolar trafficking and secretory pathways. Based on these results, I suggested that the AP-1-dependent trafficking pathway is crucial to plant development.
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