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| Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller |
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| Author(s): Miele AE, Watson PJ, Evans PR, Traub LM, Owen DJ |
| Source: NATURE STRUCTURAL & MOLECULAR BIOLOGY Volume: 11 Issue: 3 Pages: 242-248 Published: MAR 2004 |
| Times Cited: 39 References: 50 |
| Abstract: During the assembly of clathrin-coated vesicles, many peripheral membrane proteins, including the amphiphysins, use LLDLD-type clathrin-box motifs to interact with the N-terminal beta-propeller domain (TD) of clathrin. The 2.3 Angstrom resolution structure of the clathrin TD in complex with a TLPWDLWTT peptide from amphiphysin 1 delineates a second clathrin-binding motif, PWXXW ( the W box), that binds at a site on the TD remote from the clathrin box binding site. The presence of both sequence motifs within the unstructured region of the amphiphysins allows them to bind more tightly to free TDs than do other endocytic proteins that contain only clathrin-box motifs. This property, along with the propensity of the N-terminal BAR domain to bind curved membranes, will preferentially localize amphiphysin and its partner, dynamin, to the periphery of invaginated clathrin lattices. |
| Document Type: Article |
| Language: English |
| Reprint Address: Traub, LM (reprint author), Univ Pittsburgh, Sch Med, Dept Cell Biol & Physiol, Pittsburgh, PA 15261 USA |
Addresses:
1. Univ Pittsburgh, Sch Med, Dept Cell Biol & Physiol, Pittsburgh, PA 15261 USA
2. MRC, Mol Biol Lab, Cambridge CB2 2QH, England
3. Univ Cambridge, Cambridge Inst Med Res, Cambridge CB2 2XY, England |
| Publisher: NATURE PUBLISHING GROUP, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 USA |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: 804ED |
| ISSN: 1545-9985 |
| DOI: 10.1038/nsmb736 |
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