| Primary Identifier | IPR008153 | Type | Domain |
| Short Name | GAE_dom |
| description | The adaptor proteins AP-1 and GGA (Golgi-localized, gamma ear-containing, ADP-ribosylation factor (ARF)-binding proteins) regulate membrane traffic betweenthe trans-Golgi network (TGN) and endosome/lysosomes through ARF-regulatedmembrane association, recognition of sorting signals, and recruitment ofclathrin and accessory proteins. The gamma-adaptin ear (GAE) domain is a C-terminal appendage or ear of about 120 residues, which is found in gamma-adaptins, the heavy subunits of the AP-1 complex, and in GGAs. The GAE domain,which is found in associated with other domains such as VHS,coiled-coils and GAT, is involved in the recruitment of accessory proteins,such as gamma-synergin, Rababptin-5, Eps15 and cyclin G-associated kinase,which modulate the functions of GAE domain containing proteins in the membranetrafficking events [, , , ].The resolution of the 3D-structure of the human gamma-adaptin GAE domain shows that it forms an immunoglobulin-like β-sandwich fold composed of eightβ-strands with two short α-helices. The topology ofthe entire GAE domain is similar to those of the N-terminal subdomains in thealpha- and beta-adaptin ear domains of the AP-2 complex. However, the GAEdomain has very low sequence identity and homology to the N-terminalimmunoglobulin-like subdomains of the alpha and beta ear domains. The bindingsite for the accessory proteins has been located to a shallow hydrophobictrough surrounded by charged (mainly basic) residues [, ].This entry represents the entire GAE domain. |
