Properties of GST-CALM expressed in E. coli

Jeong Ah Kim, Seong Ryul Kim, Yong Keun Jung, So Youn Woo, Ju Young Seoh, Young Sook Hong, Hyung Lae Kim

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


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.

Original languageEnglish
Pages (from-to)93-99
Number of pages7
JournalExperimental and Molecular Medicine
Issue number2
StatePublished - 30 Jun 2000


  • AP180
  • CALM
  • Clathrin-coated vesicle
  • Expression
  • Regulation
  • SH3 domain


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