Properties of GST-CALM expressed in E. coli
Experimental & Molecular Medicine
; : 93-99, 2000.
Artigo
em Inglês
| WPRIM (Pacífico Ocidental)
| ID: wpr-75097
Biblioteca responsável:
WPRO
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. coli. 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.
Texto completo:
Disponível
Contexto em Saúde:
Doenças Negligenciadas
Problema de saúde:
Doenças Negligenciadas
/
Zoonoses
Base de dados:
WPRIM (Pacífico Ocidental)
Assunto principal:
Fosfoproteínas
/
Ligação Proteica
/
Proteínas Recombinantes de Fusão
/
Calpaína
/
Domínios de Homologia de src
/
Caspases
/
Vesículas Revestidas por Clatrina
/
Eletroforese em Gel de Poliacrilamida
/
Escherichia coli
/
Glutationa Transferase
Limite:
Animais
Idioma:
Inglês
Revista:
Experimental & Molecular Medicine
Ano de publicação:
2000
Tipo de documento:
Artigo