articleThe Journal of Cell BiologyOct 4, 2004BRONZE OA

XBP1

Loyola University Chicago · St. Jude Children's Research Hospital · +1 more institution

PubMed
Indexed incrossrefpubmed

Abstract

When the protein folding capacity of the endoplasmic reticulum (ER) is challenged, the unfolded protein response (UPR) maintains ER homeostasis by regulating protein synthesis and enhancing expression of resident ER proteins that facilitate protein maturation and degradation. Here, we report that enforced expression of XBP1(S), the active form of the XBP1 transcription factor generated by UPR-mediated splicing of XBP1 mRNA, is sufficient to induce synthesis of phosphatidylcholine, the primary phospholipid of the ER membrane. Cells overexpressing XBP1(S) exhibit elevated levels of membrane phospholipids, increased surface area and volume of rough ER, and enhanced activity of the cytidine diphosphocholine…

Citation impact

649
total citations
FWCI
8.93
Percentile
100%
References
34
Citations per year

Authors

4

Topics & keywords

Keywords
  • XBP1
  • Endoplasmic reticulum
  • Unfolded protein response
  • Biology
  • Cell biology
  • Protein biosynthesis
  • Biochemistry
  • RNA splicing
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Funding