Neuregulin 1-alpha regulates phosphorylation, acetylation, and alternative splicing in lymphoblastoid cells

Genome. 2013 Oct;56(10):619-25. doi: 10.1139/gen-2013-0068. Epub 2013 Jul 20.


Neuregulins (NRGs) are signaling molecules involved in various cellular and developmental processes. Abnormal expression and (or) genomic variations of some of these molecules, such as NRG1, have been associated with disease conditions such as cancer and schizophrenia. To gain a comprehensive molecular insight into possible pathways/networks regulated by NRG1-alpha, we performed a global expression profiling analysis on lymphoblastoid cell lines exposed to NRG1-alpha. Our data show that this signaling molecule mainly regulates coordinated expression of genes involved in three processes: phosphorylation, acetylation, and alternative splicing. These processes have fundamental roles in proper development and function of various tissues including the central nervous system (CNS)--a fact that may explain conditions associated with NRG1 dysregulations such as schizophrenia. The data also suggest NRG1-alpha regulates genes (FBXO41) and miRNAs (miR-33) involved in cholesterol metabolism. Moreover, RPN2, a gene already shown to be dysregulated in breast cancer cells, is also differentially regulated by NRG1-alpha treatment.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Alternative Splicing*
  • Cell Line
  • Central Nervous System / metabolism*
  • Cholesterol / metabolism
  • Gene Expression Regulation
  • Gene Ontology
  • Hexosyltransferases
  • Humans
  • MicroRNAs / metabolism
  • Neuregulin-1 / genetics
  • Neuregulin-1 / pharmacology*
  • Neuregulin-1 / physiology*
  • Phosphorylation
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Isoforms / pharmacology
  • Protein Isoforms / physiology
  • Schizophrenia / genetics*
  • Signal Transduction
  • Transcriptome


  • MIRN33a microRNA, human
  • MicroRNAs
  • Neuregulin-1
  • Protein Isoforms
  • Cholesterol
  • Hexosyltransferases
  • RPN2 protein, human
  • Proteasome Endopeptidase Complex