Molecular cloning of clathrin assembly protein gene (rCALM) and its differential expression to AP180 in rat brain.
- Author:
Hyung Lae KIM
1
;
Sunhee Cho LEE
Author Information
1. Department of Biochemistry, College of Medicine, Ewha Womans University, Seoul, Korea. hyung@mm.ewha.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
clathrin-coated vesicle;
AP180;
CALM;
gene cloning;
expression
- MeSH:
Age Factors;
Alternative Splicing;
Amino Acid Sequence;
Animal;
Base Sequence;
Brain/physiology*;
Cloning, Molecular;
Gene Expression Regulation, Developmental;
Molecular Sequence Data;
Nerve Tissue Proteins/metabolism;
Nerve Tissue Proteins/genetics*;
Phosphoproteins/metabolism;
Phosphoproteins/genetics*;
Rats;
Sequence Homology, Amino Acid
- From:Experimental & Molecular Medicine
1999;31(4):191-196
- CountryRepublic of Korea
- Language:English
-
Abstract:
Binding of clathrin assembly protein to clathrin triskelia induces their assembly into clathrin-coated vesicle (CCV) in neurons. The clathrin assembly protein gene (rCALM) was cloned from rat brain cDNA library. rCALM deduced 69 kD molecule has overall 73% amino acid homology compared with that of AP180 protein. The N-terminal domain, where amino acid sequences are very similar with AP180, harbours binding sites for clathrin and inositides, as well as possible phosphorylation sites, but the proline rich C-terminal domain is different from that of AP180. The mRNA expression of rCALM and AP180 by in situ hybridization histochemistry revealed that the rCALM mRNA was more intensely expressed than that of AP180, and the distribution patterns were different from each other. These results suggest that the rCALM mediates the assembly of clathrin in neural and supporting cells of brain, and regulates the clathrin coated-vesicle formation through phosphorylation and inositide metabolism. Copyright 2000 Academic Press.
