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- Title
Nuclear localization of clathrin involves a labile helix outside the trimerization domain
- Authors
Ybe, Joel A.; Fontaine, Sarah N.; Stone, Todd; Nix, Jay; Lin, Xiaoyan; Mishra, Sanjay
- Abstract
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.
- Subjects
CLATHRIN; TRIMERIZATION; ENDOCYTOSIS; SUBCELLULAR fractionation; CYSTEINE; MUTANT proteins
- Publication
FEBS Letters, 2013, Vol 587, Issue 2, p142
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.11.005