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Defining human ERAD networks through an integrative mapping strategy.

Nature cell biology | Nov 27, 2011

Proteins that fail to correctly fold or assemble into oligomeric complexes in the endoplasmic reticulum (ER) are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). Although many individual components of the ERAD system have been identified, how these proteins are organized into a functional network that coordinates recognition, ubiquitylation and dislocation of substrates across the ER membrane is not well understood. We have investigated the functional organization of the mammalian ERAD system using a systems-level strategy that integrates proteomics, functional genomics and the transcriptional response to ER stress. This analysis supports an adaptive organization for the mammalian ERAD machinery and reveals a number of metazoan-specific genes not previously linked to ERAD.

Pubmed ID: 22119785 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Endoplasmic Reticulum | Endoplasmic Reticulum-Associated Degradation | HEK293 Cells | HeLa Cells | Humans | Molecular Sequence Data | Proteasome Endopeptidase Complex | Protein Folding | Proteins | Proteolysis | RNA Interference | Receptors, Autocrine Motility Factor | Ubiquitin-Protein Ligases

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Associated grants

  • Agency: NIGMS NIH HHS, Id: F32 GM086026-01
  • Agency: NIGMS NIH HHS, Id: R01 GM074874-06
  • Agency: NIGMS NIH HHS, Id: F32 GM086026-02
  • Agency: NIA NIH HHS, Id: R01 AG011085
  • Agency: NIGMS NIH HHS, Id: F32 GM086026-03
  • Agency: NIGMS NIH HHS, Id: R01 GM070565
  • Agency: NINDS NIH HHS, Id: R01 NS042842-09
  • Agency: NIGMS NIH HHS, Id: F32 GM086026
  • Agency: NIGMS NIH HHS, Id: R01 GM074874
  • Agency: NIGMS NIH HHS, Id: R01 GM054137
  • Agency: NINDS NIH HHS, Id: R01 NS042842

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