Journal
MOLECULAR CELL
Volume 28, Issue 4, Pages 544-554Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2007.09.012
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Funding
- NCI NIH HHS [CA21765, P30 CA021765] Funding Source: Medline
- NIGMS NIH HHS [GM54068, R01 GM054068-12, R01 GM054068] Funding Source: Medline
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To investigate the disposal of nonglycosylated BiP substrates, we used a nonsecreted kappa LC, which exists in partially (ox1) and completely (ox2) oxidized states. The ox2 form is partially reduced in order to be degraded, and only the ox1 form is ubiquitinated and associates with both Herp and Derlin-1. Herp is in a complex with ubiquitinated proteins and with the 26S proteasome, suggesting that it plays a role in linking substrates with the proteasome. Over-expressed Herp also interacts with two other BiP substrates, but not with two calnexin substrates. Either expression of p97 or Hrd1 mutants, which are in a complex with Herp and Derlin-1, or reduction of Herp levels inhibited the degradation of the BiP substrates, whereas the latter had no effect on the degradation of the calnexin substrates. This result suggests that there is some distinction in the pathways used to dispose of these two types of ERAD substrates.
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