Characterization of Interaction Between Clathrin Light and Heavy Chains in <I>Arabidopsis</I>
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- Nishimura Kohji
- Cent. Integ. Res. Sci., Shimane Univ.
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- Ishikawa Syouta
- Fac. Life Env. Sci., Shimane Univ.
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- Yamauchi Junji
- Dept. Pharmacol., Natl. Res. Inst. Child Hlth. Dev.
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- Hattori Sayoko
- Fac. Life Env. Sci., Shimane Univ.
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- Nakagawa Tsuyoshi
- Cent. Integ. Res. Sci., Shimane Univ.
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- Jisaka Mitsuo
- Fac. Life Env. Sci., Shimane Univ.
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- Nagaya Tsutomu
- Fac. Life Env. Sci., Shimane Univ.
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- Yokota Kazushige
- Fac. Life Env. Sci., Shimane Univ.
Bibliographic Information
- Other Title
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- シロイヌナズナのクラスリン軽鎖と重鎖の相互作用の解析
Abstract
Clathrin is a coat protein of a clathrin-coated vesicle (CCV), which sorts cargo proteins into various endosomes from trans-Golgi network and plasma membrane in mammalian, yeast and plant cells. The clathrin coat is composed of a microscopically visible structure with tree-legged shape, called triskelion. This triskelion comprises three clathrin heavy chains (CHCs), each harboring a single clathrin light chain (CLC). CHCs are well conserved among eukaryotic cells while CLCs vary in similarity, suggesting the latter may have an organism-specific function, but an interaction between CLC and CHC in Arabidopsis thaliana has not been analyzed in detail. In this study, the interaction of both types of Arabidopsis clathrin molecules was analyzed. Yeast two-hybrid and bimolecular fluorescence complementation analyses revealed Arabidopsis CLC actually interacted with CHC. Deletion analysis of CLC (1-258) showed an internal region of CLC (82-144) interacted with hub of CHC (1086-1705), suggesting the similar tendency of interaction of plant clathrin chains to that in mammalian cells. The analysis of the interaction of Arabidopsis CLC and CHC molecules will be discussed in this presentation,
Journal
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- Plant and Cell Physiology Supplement
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Plant and Cell Physiology Supplement 2011 (0), 0111-0111, 2011
The Japanese Society of Plant Physiologists
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Details 詳細情報について
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- CRID
- 1390001205632929920
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- NII Article ID
- 130006994870
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed