| First Author | Ritter B | Year | 2003 |
| Journal | EMBO Rep | Volume | 4 |
| Issue | 11 | Pages | 1089-95 |
| PubMed ID | 14555962 | Mgi Jnum | J:114134 |
| Mgi Id | MGI:3688370 | Doi | 10.1038/sj.embor.embor7400004 |
| Citation | Ritter B, et al. (2003) Identification of a family of endocytic proteins that define a new alpha-adaptin ear-binding motif. EMBO Rep 4(11):1089-95 |
| abstractText | Endocytosis by clathrin-coated vesicles (CCVs) is an important mechanism mediating protein internalization. Here, we show that two proteins identified through a proteomics analysis of CCVs are new components of the endocytic machinery. The proteins, named NECAP (adaptin-ear-binding coat-associated protein) 1 and 2, are paralogues that display no sequence similarity or common domains with any known protein. Both are enriched in CCV coats, and further analysis of the brain-enriched isoform, NECAP 1, shows its partial localization to clathrin-coated pits and direct binding to the globular ear domain of the alpha-adaptin subunit (alpha-ear) of the adaptor protein 2 (AP-2) complex. Intriguingly, this interaction is mediated by a new motif, WVQF, that uses a distinct alpha-ear interface relative to known alpha-ear-binding partners. Disruption of this interaction blocks clathrin-mediated endocytosis. Together, our studies identify a new family of endocytic proteins that define a unique AP-2-binding motif. |
