Nuclear localization of clathrin involves a labile helix outside the trimerization domain
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Updated: May 16, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
Joel A Ybe1, Sarah N Fontaine, Todd Stone
1Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, 212 S. Hawthorne Drive, Bloomington, IN 47405, USA. jybe@indiana.edu
Abstract:
Clathrin is a trimeric protein involved in receptor-mediated-endocytosis, but can function as a non-trimer outside of endocytosis. We have discovered that the subcellular distribution of a clathrin cysteine mutant we previously studied is altered and a proportion is also localized to nuclear spaces. MALS shows C1573A hub is a mixture of trimer-like and detrimerized molecules. The X-ray structure of the trimerization domain reveals that without light chains, a helix harboring cysteine-1573 is reoriented. We propose clathrin has a detrimerization switch, which suggests clathrin topology can be altered naturally for new functions.
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