Submit Data |  Help |  Video Tutorials |  News |  Publications |  FTP Download |  REST API |  Citing RGD |  Contact   

Identification of a family of endocytic proteins that define a new alpha-adaptin ear-binding motif.

Authors: Ritter, B  Philie, J  Girard, M  Tung, EC  Blondeau, F  McPherson, PS 
Citation: Ritter B, etal., EMBO Rep 2003 Nov;4(11):1089-95. Epub 2003 Oct 10.
Pubmed: (View Article at PubMed) PMID:14555962
DOI: Full-text: DOI:10.1038/sj.embor.embor7400004

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.


Objects referenced in this article

Additional Information

RGD Object Information
RGD ID: 1302822
Created: 2004-10-25
Species: All species
Last Modified: 2006-04-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.