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Properties of GST-CALM expressed in E-coli
- Title
- Properties of GST-CALM expressed in E-coli
- Authors
- Kim, JA; Kim, SR; Jung, YK; Woo, SY; Seoh, JY; Hong, YS; Kim, HL
- Ewha Authors
- 홍영숙; 서주영; 김형래; 우소연
- SCOPUS Author ID
- 홍영숙; 서주영; 김형래; 우소연
- Issue Date
- 2000
- Journal Title
- EXPERIMENTAL AND MOLECULAR MEDICINE
- ISSN
- 1226-3613
- Citation
- EXPERIMENTAL AND MOLECULAR MEDICINE vol. 32, no. 2, pp. 93 - 99
- Keywords
- expression; clathrin-coated vesicle; CALM; AP180; regulation; SH3 domain
- Publisher
- KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
- Indexed
- SCI; SCIE; SCOPUS; KCI
- Document Type
- Article
- Abstract
- Clathrin-coated vesicles (CCVs) are involved in protein and lipid trafficking between intracellular compartments in eukaryotic cells. CCVs are composed of clathrin and assembly proteins, The clathrin assembly protein lymphoid myeloid leukemia (CALM) gene, encodes a homologoue of the neuronal clathrin assembly protein AP180. In this study, we characterized the properties of the CALM expressed in E. coil. The molecular weight of bacterially expressed GST-CALM fusion protein was approximately 105 kD on SDS-PAGE, The CALM protein could promote clathrin triskelia into clathrin cages and could bind the preformed clathrin cage. However, 33 kD N-terminal domain of CALM could not bind pre-assembled clathrin cages, but assemble clathrin triskelia into clathrin cages. The CALM protein was bound to SH3 domain through N-terminal domain1, in vitro. The CALM protein is proteolyzed by caspase 3, caspase 8 and calpain through C-terminal domain.
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- 의과대학 > 의학과 > Journal papers
- Files in This Item:
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