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Defining human ERAD networks through an integrative mapping strategy.

  • Author(s): Christianson, John
  • Olzmann, James
  • Shaler, Thomas
  • Sowa, Mathew
  • Bennett, Eric
  • Richter, Caleb
  • Tyler, Ryan
  • Greenblatt, Ethan
  • Harper, J
  • Kopito, Ron
  • et al.

Published Web Location

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.

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