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Properties of GST-CALM expressed in E. coli

descriptionPublicationkeyboard_double_arrow_right Article 01 Jun 2000Publisher:Springer Science and Business Media LLCJournal:Experimental & Molecular Medicine, volume 32, pages 93-99 (eissn: 2092-6413,

Authors: Young Sook Hong; Jeong Ah Kim; Hyung Lae Kim; Yong-Keun Jung; So Youn Woo; Seong Ryul Kim; Ju Young Seoh;

doi: 10.1038/emm.2000.17

pmid: 10926122

Properties of GST-CALM expressed in E. coli

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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.

Related Organizations

Chungbuk National University
Korea (Republic of)
Ewha Womans University
Korea (Republic of)
Gwangju Institute of Science and Technology
Korea (Republic of)

Keywords

Caspase 8, Mice, Inbred BALB C, Calpain, Caspase 3, Antibodies, Monoclonal, Clathrin-Coated Vesicles, Nerve Tissue Proteins, Phosphoproteins, Caspase 9, Adaptor Proteins, Vesicular Transport, Mice, Caspases, Monomeric Clathrin Assembly Proteins, Escherichia coli, Animals, Electrophoresis, Polyacrylamide Gel, Female, Rabbits, Glutathione Transferase, Protein Binding

7 Research products, page 1 of 1

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