Pro-apoptotic ASY/Nogo-B protein associates with ASYIP

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Updated: Sep 25, 2026

Detection and Isolation of Apoptotic Bodies to High Purity
12:17

Detection and Isolation of Apoptotic Bodies to High Purity

Published on: August 12, 2018

Bing Qi1, Yipeng Qi, Akihiro Watari

  • 1Institute of Virology, Wuhan University, Wuhan, Hubei, Peoples Republic of China.

Journal of Cellular Physiology
|June 18, 2003
PubMed

Insights

Researchers identified ASYIP, a protein interacting with ASY/Nogo-B. ASYIP, also known as RTN3, interacts with ASY/Nogo-B and is localized in the endoplasmic reticulum, potentially clarifying cancer apoptosis and neuronal regeneration mechanisms.

Area of Science:

  • Molecular Biology
  • Neuroscience
  • Cancer Research

Background:

  • Ectopic expression of ASY/Nogo-B induces apoptosis in cancer cells.
  • Nogo-A, an ASY splice variant, inhibits neuronal regeneration in the central nervous system.

Purpose of the Study:

  • To investigate the mechanism of ASY-induced apoptosis and Nogo-A-mediated inhibition of neuronal regeneration.
  • To identify and characterize proteins that interact with ASY.

Main Methods:

  • Yeast two-hybrid screening to identify ASY-interacting proteins.
  • Cloning and sequencing of the ASY-interacting protein (ASYIP).
  • Mutational analysis, immunofluorescence, and co-localization studies.

Main Results:

  • Identified and cloned ASYIP, a protein identical to reticulon 3 (RTN3).
  • ASYIP contains two hydrophobic regions and an ER retrieval motif.
  • ASY and ASYIP form a complex in human cells, requiring ASYIP's hydrophobic regions for association.
  • ASYIP co-localizes with ASY in the endoplasmic reticulum.

Conclusions:

  • ASYIP (RTN3) interacts with ASY/Nogo-B.
  • The interaction occurs in the endoplasmic reticulum.
  • Understanding ASYIP's function may elucidate mechanisms of cancer cell apoptosis and neuronal regeneration inhibition.

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