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Cleavage of purified neuronal clathrin assembly protein (CALM) by caspase 3 and calpain

Title
Cleavage of purified neuronal clathrin assembly protein (CALM) by caspase 3 and calpain
Authors
Kim, JAKim, HL
Ewha Authors
김형래
SCOPUS Author ID
김형래scopus
Issue Date
2001
Journal Title
EXPERIMENTAL AND MOLECULAR MEDICINE
ISSN
1226-3613JCR Link
Citation
vol. 33, no. 4, pp. 245 - 250
Keywords
clathrin-coated vesicleCALMcaspaseexpression
Publisher
KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
Indexed
SCI; SCIE; SCOPUS; KCI WOS scopus
Abstract
The most efficient means of protein internalization from the membrane are through clathrin-coated pits, which concentrate protein interactions with the clathrin-associated assembly protein complex AP-2 and internalization signals in the cytoplasmic domain of transmembrane proteins. Binding of clathrin assembly protein to clathrin triskelia induces their assembly into clathrin-coated vesicles (CCVs). Due to a difficulty of isolating clathrin molecules from their complex or assembly state in the cells, most of the studies were carried out with recombinant clathrin proteins, which may present different conformation and structural variation. In this study, we have developed an efficient method of isolating the native clathrin assembly protein lymphoid myeloid (CALM) from the bovine brain that is enriched with clathrin and clathrin associated proteins and characterized by their sensitivity to proteases and it's ability to form CCV. The purified CALM has molecular weight of approximately 100,000 dalton on SDS-PAGE, which is consistent with the result of in vitro translation. The purified CALM protein could promote the assembly of clathrin triskelia into clathrin cage, and cleaved CALM proteolysed by caspase 3 and calpain could not promote them. In this respect, our data support a model in which CALM functions like AP180 as a monomeric clathrin assembly protein and might take part in apoptotic process in neuronal cells.
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의과대학 > 의학과 > Journal papers
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