Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain.
The adaptor proteins AP-1 and GGA regulate membrane traffic between the trans-Golgi network (TGN) and endosomes/lysosomes through ARF-regulated membrane association, recognition of sorting signals, and recruitment of clathrin and accessory proteins. The gamma 1-adaptin subunits of AP-1 and GGA possess homologous ear domains involved in the recruitment of accessory proteins, gamma-synergin and Rabaptin-5. The crystal structure of the human gamma 1-adaptin ear domain consists solely of an immunoglobulin-like fold, unlike the alpha-adaptin ear domain. Structure-based mutational analyses reveal a binding site for the accessory proteins that is composed of conserved basic residues, indicating that the recruitment mechanism in gamma 1-adaptin and GGA is distinct from that in alpha-adaptin.
Nogi
Terukazu
T
Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki 305-0801, Japan.
Shiba
Yoko
Y
Kawasaki
Masato
M
Shiba
Tomoo
T
Matsugaki
Naohiro
N
Igarashi
Noriyuki
N
Suzuki
Mamoru
M
Kato
Ryuichi
R
Takatsu
Hiroyuki
H
Nakayama
Kazuhisa
K
Wakatsuki
Soichi
S
D033982:Adaptor Protein Complex gamma Subunits; D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D020798:Two-Hybrid System Techniques
D033982:Adaptor Protein Complex gamma Subunits; D008565:Membrane Proteins; D021122:Protein Subunits