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

Author

Listed:
  • Tomoo Shiba

    (Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
    Foundation for Advancement of International Science (FAIS))

  • 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))

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.

Suggested Citation

  • Tomoo Shiba & Hiroyuki Takatsu & Terukazu Nogi & Naohiro Matsugaki & Masato Kawasaki & Noriyuki Igarashi & Mamoru Suzuki & Ryuichi Kato & Thomas Earnest & Kazuhisa Nakayama & Soichi Wakatsuki, 2002. "Structural basis for recognition of acidic-cluster dileucine sequence by GGA1," Nature, Nature, vol. 415(6874), pages 937-941, February.
    • Handle: RePEc:nat:nature:v:415:y:2002:i:6874:d:10.1038_415937a
    DOI: 10.1038/415937a
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