Structural basis for recognition of acidic-cluster dileucine sequence by GGA1

Tomoo Shiba, Hiroyuki Takatsu, Terukazu Nogi, Naohiro Matsugaki, Masato Kawasaki, Noriyuki Igarashi, Mamoru Suzuki, Ryuichi Kato, Thomas Earnest, Kazuhisa Nakayama and Soichi Wakatsuki ()
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Tomoo Shiba: Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Hiroyuki Takatsu: Institute of Biological Sciences and Gene Research Center, University of Tsukuba
Terukazu Nogi: Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Naohiro Matsugaki: Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Masato Kawasaki: Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Noriyuki Igarashi: Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Mamoru Suzuki: Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Ryuichi Kato: Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Thomas Earnest: Advanced Light Source, Berkeley, Berkeley Center for Structural Biology, Lawrence Berkeley National Laboratory
Kazuhisa Nakayama: Institute of Biological Sciences and Gene Research Center, University of Tsukuba
Soichi Wakatsuki: Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)

Nature, 2002, vol. 415, issue 6874, 937-941

Abstract: Abstract GGAs (Golgi-localizing, γ-adaptin ear homology domain, ARF-interacting proteins) are critical for the transport of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF), and clathrin1,2. The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster dileucine (ACLL) sequences1,2,3,4,5,6. Here we report the X-ray structure of the GGA1 VHS domain alone, and in complex with the carboxy-terminal peptide of cation-independent mannose 6-phosphate receptor containing an ACLL sequence. The VHS domain forms a super helix with eight α-helices, similar to the VHS domains of TOM1 and Hrs. Unidirectional movements of helices α6 and α8, and some of their side chains, create a set of electrostatic and hydrophobic interactions for correct recognition of the ACLL peptide. This recognition mechanism provides the basis for regulation of protein transport from the TGN to endosomes/lysosomes, which is shared by sortilin and low-density lipoprotein receptor-related protein.

Date: 2002
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DOI: 10.1038/415937a

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