Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains

Han Seok Ko, Takashi Uehara, Kazuhiro Tsuruma, Yasuyuki Nomura

Research output: Contribution to journalArticle

115 Citations (Scopus)

Abstract

Mammalian cells acquire tolerance against multiple stressors through the high-level expression of stress-responsible genes. We have previously demonstrated that protein-disulfide isomerase (PDI) together with ubiquilin are up-regulated in response to hypoxia/brain ischemia, and play critical roles in resistance to these damages. We show here that ubiquilin interacts preferentially with poly-ubiquitin chains and 19S proteasome subunits. Taken together, these results suggest that ubiquitin could serve as an adaptor protein that both interacts with PDI and mediates the delivery of poly-ubiquitylated proteins to the proteasome in the cytosol in the vicinity of the endoplasmic reticulum membrane.

Original languageEnglish
Pages (from-to)110-114
Number of pages5
JournalFEBS Letters
Volume566
Issue number1-3
DOIs
Publication statusPublished - May 21 2004
Externally publishedYes

Keywords

  • ER, endoplasmic reticulum
  • ERAD, ER-associated degradation
  • NP, asparagine-proline repeats
  • UBA, ubiquitin-associated
  • UBA52, ubiquitin amino acid 52-residue ribosomal protein fusion
  • UBL, ubiquitin-like
  • UPR, unfolded protein response
  • Ub, ubiquitin

ASJC Scopus subject areas

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

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