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- Title
Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain.
- Authors
Nogi, Terukazu; Shiba, Yoko; Kawasaki, Masato; Shiba, Tomoo; Matsugaki, Naohiro; Igarashi, Noriyuki; Suzuki, Mamoru; Kato, Ryuichi; Takatsu, Hiroyuki; Nakayama, Kazuhisa; Wakatsuki, Soichi
- Abstract
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.
- Publication
Nature structural biology, 2002, Vol 9, Issue 7, p527
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/nsb808