Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress

J Biol Chem. 2000 Oct 20;275(42):32846-53. doi: 10.1074/jbc.M002063200.

Abstract

Hyperhomocysteinemia, a risk factor for vascular disease, injures endothelial cells through undefined mechanisms. We previously identified several homocysteine-responsive genes in cultured human vascular endothelial cells, including the endoplasmic reticulum (ER)-resident molecular chaperone GRP78/BiP. Here, we demonstrate that homocysteine induces the ER stress response and leads to the expression of a novel protein, Herp, containing a ubiquitin-like domain at the N terminus. mRNA expression of Herp was strongly up-regulated by inducers of ER stress, including mercaptoethanol, tunicamycin, A23187, and thapsigargin. The ER stress-dependent induction of Herp was also observed at the protein level. Immunochemical analyses using Herp-specific antibodies indicated that Herp is a 54-kDa, membrane-associated ER protein. Herp is the first integral membrane protein regulated by the ER stress response pathway. Both the N and C termini face the cytoplasmic side of the ER; this membrane topology makes it unlikely that Herp acts as a molecular chaperone for proteins in the ER, in contrast to GRP78 and other ER stress-responsive proteins. Herp may, therefore, play an unknown role in the cellular survival response to stress.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Calcimycin / pharmacology
  • Cells, Cultured
  • Cloning, Molecular
  • Endoplasmic Reticulum / drug effects
  • Endoplasmic Reticulum / physiology*
  • Endoplasmic Reticulum Chaperone BiP
  • Endothelium, Vascular / drug effects
  • Endothelium, Vascular / physiology*
  • Gene Expression Regulation / drug effects
  • Gene Expression Regulation / physiology*
  • Humans
  • Intracellular Membranes / physiology
  • Intracellular Membranes / ultrastructure
  • Membrane Proteins / biosynthesis
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics*
  • Mercaptoethanol / pharmacology
  • Mice
  • Molecular Sequence Data
  • Protein Biosynthesis
  • Protein Conformation
  • RNA, Messenger / genetics
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Thapsigargin / pharmacology
  • Transcription, Genetic* / drug effects
  • Tunicamycin / pharmacology
  • Ubiquitins / chemistry*
  • Umbilical Veins

Substances

  • Endoplasmic Reticulum Chaperone BiP
  • HERPUD1 protein, human
  • HSPA5 protein, human
  • Herpud1 protein, mouse
  • Hspa5 protein, mouse
  • Membrane Proteins
  • RNA, Messenger
  • Recombinant Proteins
  • Ubiquitins
  • Tunicamycin
  • Calcimycin
  • Mercaptoethanol
  • Thapsigargin

Associated data

  • GENBANK/AB034989
  • GENBANK/AB034991