Structural highlights
Function
[CLH1_BOVIN] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.
Publication Abstract from PubMed
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.
Nuclear localization of clathrin involves a labile helix outside the trimerization domain.,Ybe JA, Fontaine SN, Stone T, Nix J, Lin X, Mishra S FEBS Lett. 2013 Jan 16;587(2):142-9. doi: 10.1016/j.febslet.2012.11.005. Epub, 2012 Nov 21. PMID:23178717[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ybe JA, Fontaine SN, Stone T, Nix J, Lin X, Mishra S. Nuclear localization of clathrin involves a labile helix outside the trimerization domain. FEBS Lett. 2013 Jan 16;587(2):142-9. doi: 10.1016/j.febslet.2012.11.005. Epub, 2012 Nov 21. PMID:23178717 doi:10.1016/j.febslet.2012.11.005
