{Reference Type}: Journal Article
{Title}: Definition of the consensus motif recognized by gamma-adaptin ear domains.
{Author}: Mattera R;Ritter B;Sidhu SS;McPherson PS;Bonifacino JS;
{Journal}: J Biol Chem
{Volume}: 279
{Issue}: 9
{Year}: Feb 2004 27
暂无{DOI}: 10.1074/jbc.M311873200
{Abstract}: The heterotetrameric adaptor complex 1 (AP-1) and the monomeric Golgi-localized, gamma ear-containing, Arf-binding (GGA) proteins are components of clathrin coats associated with the trans-Golgi network and endosomes. The carboxyl-terminal ear domains (or gamma-adaptin ear (GAE) domains) of two gamma-adaptin subunit isoforms of AP-1 and of the GGAs are structurally similar and bind to a common set of accessory proteins. In this study, we have systematically defined a core tetrapeptide motif PsiG(P/D/E)(Psi/L/M) (where Psi is an aromatic residue), which is responsible for the interactions of accessory proteins with GAE domains. The definition of this motif has allowed us to identify novel GAE-binding partners named NECAP and aftiphilin, which also contain clathrin-binding motifs. These findings shed light on the mechanism of accessory protein recruitment to trans-Golgi network and endosomal clathrin coats.