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The calcium-binding site of clathrin light chains
1Department of Pharmacy, School of Pharmacy, University of California, San Francisco 94143.
The Journal of Biological Chemistry
|October 25, 1990
Summary
Calcium binding by clathrin light chains regulates vesicle assembly. This study identifies a specific calcium-binding site in light chains, revealing the structural basis for calcium
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Clathrin light chains are calcium-binding proteins.
- Clathrin assembly is modulated by calcium in vitro, suggesting a regulatory role for intracellular calcium in clathrin-coated vesicle function.
Purpose of the Study:
- To define the structural basis for calcium's influence on clathrin-mediated processes.
- To investigate the calcium-binding properties of clathrin light chains.
Main Methods:
- Utilized recombinant deletion mutants of clathrin light chains.
- Employed isolated fragments of clathrin light chains.
- Analyzed the calcium-binding site structure and its similarity to known calcium-binding motifs.
Main Results:
- Identified a single calcium-binding site (residues 85-96) in mammalian (LCa, LCb) and yeast light chains.
- This site shares structural similarity with EF-hand loops found in calmodulin.
- In mammalian light chains, the calcium-binding sequence is adjacent to domains controlling clathrin assembly and disassembly.
Conclusions:
- Calcium binding to clathrin light chains likely plays a regulatory role in clathrin-coated vesicle dynamics.
- The identified EF-hand-like motif provides a structural explanation for calcium's effect on clathrin assembly and disassembly.