Involvement of the IRE1α-XBP1 pathway and XBP1s-dependent transcriptional reprogramming in metabolic diseases

DNA Cell Biol. 2015 Jan;34(1):6-18. doi: 10.1089/dna.2014.2552.

Abstract

The X-box binding protein 1 (XBP1) is not only an important component of the unfolded protein response (UPR), but also an important nuclear transcription factor. Upon endoplasmic reticulum stress, XBP1 is spliced by inositol-requiring enzyme 1 (IRE1), thereby generating functional spliced XBP1 (XBP1s). XBP1s functions by translocating into the nucleus to initiate transcriptional programs that regulate a subset of UPR- and non-UPR-associated genes involved in the pathophysiological processes of various diseases. Recent reports have implicated XBP1 in metabolic diseases. This review summarizes the effects of XBP1-mediated regulation on lipid metabolism, glucose metabolism, obesity, and atherosclerosis. Additionally, for the first time, we present XBP1s-dependent transcriptional reprogramming in metabolic diseases under different conditions, including pathology and physiology. Understanding the function of XBP1 in metabolic diseases may provide a basic knowledge for the development of novel therapeutic targets for ameliorating these diseases.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cardiovascular Diseases / metabolism
  • DNA-Binding Proteins / metabolism*
  • Diabetes Mellitus, Type 2 / metabolism*
  • Endoplasmic Reticulum Stress
  • Endoribonucleases / metabolism*
  • Gene Expression Regulation
  • Glucose / metabolism
  • Humans
  • Lipid Metabolism
  • Obesity / metabolism*
  • Protein Serine-Threonine Kinases / metabolism*
  • Regulatory Factor X Transcription Factors
  • Transcription Factors / metabolism*
  • Transcription, Genetic
  • Unfolded Protein Response
  • X-Box Binding Protein 1

Substances

  • DNA-Binding Proteins
  • Regulatory Factor X Transcription Factors
  • Transcription Factors
  • X-Box Binding Protein 1
  • XBP1 protein, human
  • ERN1 protein, human
  • Protein Serine-Threonine Kinases
  • Endoribonucleases
  • Glucose