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Related Experiment Video

Updated: Nov 7, 2025

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
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Defining the Caprin-1 Interactome in Unstressed and Stressed Conditions.

Lucas Vu1, Asmita Ghosh2,3, Chelsea Tran1,4

  • 1Department of Neurobiology, Barrow Neurological Institute, Phoenix, Arizona 85013-4409, United States.

Journal of Proteome Research
|May 3, 2021
PubMed
Summary
This summary is machine-generated.

This study reveals the protein interactome of Caprin-1, identifying novel components of cytoplasmic stress granules (SGs). A key finding is the presence of SNRNP200 in SGs and its association with cytoplasmic aggregates in amyotrophic lateral sclerosis (ALS).

Keywords:
Caprin-1RNA binding proteinsamyotrophic lateral sclerosiscytoplasmic granulescytoplasmic inclusionsmass spectrometryprotein−protein interactionsproteomicsstress granules

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Area of Science:

  • Cell Biology
  • Neuroscience
  • Proteomics

Background:

  • Cytoplasmic stress granules (SGs) are dynamic cellular structures involved in stress response.
  • SGs are implicated in neurodegenerative diseases, but their full proteome is not yet characterized.
  • Previous studies focused on G3BP1, necessitating exploration of other RNA-binding proteins (RBPs).

Purpose of the Study:

  • To comprehensively identify the protein interactome of Caprin-1, an RBP involved in mRNP granules.
  • To discover novel components of cytoplasmic stress granules.
  • To investigate the role of SG proteins in neurodegenerative diseases like ALS.

Main Methods:

  • Immunoprecipitation coupled with mass spectrometry (IP-MS) of endogenous Caprin-1.
  • Proteomic analysis to identify Caprin-1 interactors under stressed conditions.
  • Validation of identified interactors using cellular stress models and patient-derived tissues.

Main Results:

  • Identified 1543 proteins interacting with Caprin-1, enriched in ribosome, spliceosome, and RNA transport pathways.
  • Validated ANKHD1, TALIN-1, GEMIN5, and SNRNP200 as Caprin-1 interactors in arsenite-induced SGs.
  • Confirmed SNRNP200 localization to SGs under various stress conditions and its presence in cytoplasmic aggregates in ALS patient neurons.

Conclusions:

  • This study provides the first comprehensive Caprin-1 interactome, expanding our understanding of the SG proteome.
  • Novel cytoplasmic SG components, including SNRNP200, were identified.
  • The findings link SG proteins to neurodegeneration by identifying SNRNP200 in ALS patient aggregates.