Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain

Masato Akutsu, Masato Kawasaki, Yohei Katoh, Tomoo Shiba, Yoshiki Yamaguchi, Ryuichi Kato, Koichi Kato, Kazuhisa Nakayama, Soichi Wakatsuki

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)

Abstract

Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices α1 and α2. NMR and biochemical data revealed that the N-terminal half of helix α3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1.

Original languageEnglish
Pages (from-to)5385-5391
Number of pages7
JournalFEBS Letters
Volume579
Issue number24
DOIs
Publication statusPublished - 2005 Oct 10
Externally publishedYes

Keywords

  • GGA and Tom1
  • Golgi-localizing, γ-adaptin ear domain homology, ARF-binding
  • Protein transport
  • Target of Myb1
  • Ubiquitin recognition

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint

Dive into the research topics of 'Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain'. Together they form a unique fingerprint.

Cite this