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.
Mesh Terms:
Adaptor Protein Complex gamma Subunits, Amino Acid Sequence, Binding Sites, Conserved Sequence, Crystallography, X-Ray, Humans, Hydrophobicity, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Mutation, Protein Binding, Protein Structure, Tertiary, Protein Subunits, Structure-Activity Relationship, Substrate Specificity, Two-Hybrid System Techniques
Adaptor Protein Complex gamma Subunits, Amino Acid Sequence, Binding Sites, Conserved Sequence, Crystallography, X-Ray, Humans, Hydrophobicity, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Mutation, Protein Binding, Protein Structure, Tertiary, Protein Subunits, Structure-Activity Relationship, Substrate Specificity, Two-Hybrid System Techniques
Nat. Struct. Biol.
Date: Jul. 01, 2002
PubMed ID: 12042876
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