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Properties of GST-CALM expressed in E-coli

Title
Properties of GST-CALM expressed in E-coli
Authors
Kim, JAKim, SRJung, YKWoo, SYSeoh, JYHong, YSKim, HL
Ewha Authors
홍영숙서주영김형래우소연
SCOPUS Author ID
홍영숙scopusscopus; 서주영scopus; 김형래scopus; 우소연scopus
Issue Date
2000
Journal Title
EXPERIMENTAL AND MOLECULAR MEDICINE
ISSN
1226-3613JCR Link
Citation
vol. 32, no. 2, pp. 93 - 99
Keywords
expressionclathrin-coated vesicleCALMAP180regulationSH3 domain
Publisher
KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
Indexed
SCI; SCIE; SCOPUS; KCI WOS scopus
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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의학전문대학원 > 의학과 > Journal papers
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