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Structural insights into the clathrin coat
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Young, Anna. (2007) Structural insights into the clathrin coat. Seminars in Cell and Developmental Biology, Vol.18 (No.4). pp. 448-458. ISSN 1084-9521
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Official URL: http://dx.doi.org/10.1016/j.semcdb.2007.07.006
Abstract
Clathrin is a cytoplasmic protein best known for its role in endocytosis and intracellular trafficking. The diverse nature of clathrin has recently become apparent, with strong evidence available suggesting roles in both chromosome segregation and reassembly of the Golgi apparatus during mitosis. Clathrin functions as a heterohexamer, adopting a three-legged triskelion structure of three clathrin light chains and three heavy chains. During endocytosis clathrin forms a supportive network about the invaginating membrane, interacting with itself and numerous adapter proteins. Advances in the field of structural biology have led us to a greater understanding of clathrin in its assembled state, the clathrin lattice. Combining techniques such as X-ray crystallography, NMR, and cryo-electron microscopy has allowed us to piece together the intricate nature of clathrincoated vesicles and the interactions of clathrin with its many binding partners. In this review I outline the roles of clathrin within the cell and the recent structural advances that have improved our understanding of clathrin-clathrin and clathrin-protein interactions. (c) 2007 Elsevier Ltd. All rights reserved.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QH Natural history > QH301 Biology |
| Divisions: | Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010) |
| Journal or Publication Title: | Seminars in Cell and Developmental Biology |
| Publisher: | Academic Press Ltd. |
| ISSN: | 1084-9521 |
| Date: | August 2007 |
| Volume: | Vol.18 |
| Number: | No.4 |
| Number of Pages: | 11 |
| Page Range: | pp. 448-458 |
| Identification Number: | 10.1016/j.semcdb.2007.07.006 |
| Status: | Peer Reviewed |
| Publication Status: | Published |
| Access rights to Published version: | Restricted or Subscription Access |
| URI: | http://wrap.warwick.ac.uk/id/eprint/31275 |
Data sourced from Thomson Reuters' Web of Knowledge
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