Determination of topological structure of ARL6ip1 in cells: Identification of the essential binding region of ARL6ip1 for conophylline

Masahiro Kuroda, Shintaro Funasaki, Tsuyoshi Saitoh, Yukiko Sasazawa, Shigeru Nishiyama, Kazuo Umezawa, Siro Simizu

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

Conophylline (CNP) has various biological activities, such as insulin production. A recent study identified ADP-ribosylation factor-like 6-interacting protein 1 (ARL6ip1) as a direct target protein of CNP. In this study, we revealed that ARL6ip1 is a three-spanning transmembrane protein and determined the CNP-binding domain of ARL6ip1 by deletion mutation analysis of ARL6ip1 with biotinyl-amino-CNP. These results suggest that CNP is expected to be useful for future investigation of ARL6ip1 function in cells. Because of the anti-apoptotic function of ARL6ip1, CNP may be an effective therapeutic drug and/or a novel chemosensitizer for human cancers and other diseases.

Original languageEnglish
Pages (from-to)3656-3660
Number of pages5
JournalFEBS Letters
Volume587
Issue number22
DOIs
Publication statusPublished - 2013 Nov 15

Keywords

  • ARL6ip1
  • Conophylline
  • Redox-sensitive luciferase assay
  • Topology

ASJC Scopus subject areas

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

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