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Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
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Dynamic O-GlcNAcylation of Sec23-interacting protein regulates COPII function.

Tetsuya Hirata1, Quyen Nguyen1, Coco Liu1

  • 1Department of Biochemistry, Duke University School of Medicine.

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|December 25, 2025
PubMed
Summary
This summary is machine-generated.

O-linked N-acetylglucosamine (O-GlcNAc) glycosylation of Sec23-interacting protein (Sec23IP) is crucial for regulating protein transport via COPII vesicles. This modification fine-tunes Sec23IP

Keywords:
COPIIER exit siteO-GlcNAcylationSec23IPSec31Aglycosylationprotein transport

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The secretory pathway is vital for eukaryotic protein trafficking.
  • Coat protein complex II (COPII) mediates ER-to-Golgi transport via vesicles.
  • Sec23-interacting protein (Sec23IP) links COPII inner and outer coats.

Purpose of the Study:

  • To investigate the role of O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation in regulating Sec23IP function.
  • To understand how O-GlcNAc modification impacts COPII vesicle formation and protein transport.

Main Methods:

  • Validation of Sec23IP as an O-GlcNAcylated protein.
  • Rescue experiments using a mutant Sec23IP deficient in glycosylation.
  • Analysis of Sec23IP interaction with Sec31A during protein transport.

Main Results:

  • O-GlcNAcylation of Sec23IP is essential for protein transport and Sec31A recruitment to ER exit sites (ERES).
  • O-GlcNAcylation levels of Sec23IP increase during transport.
  • Increased O-GlcNAcylation reduces Sec23IP's interaction with Sec31A.

Conclusions:

  • Site-specific O-GlcNAcylation of Sec23IP spatiotemporally regulates its interaction with Sec31A.
  • This modulation fine-tunes ER exit site recruitment and COPII assembly/disassembly.
  • O-GlcNAc modification may govern COPII vesicle dynamics.