Ontology highlight
ABSTRACT:
SUBMITTER: Nakatsukasa K
PROVIDER: S-EPMC2219389 | biostudies-literature | 2008 Jan
REPOSITORIES: biostudies-literature
Nakatsukasa Kunio K Huyer Gregory G Michaelis Susan S Brodsky Jeffrey L JL
Cell 20080101 1
It remains unclear how misfolded membrane proteins are selected and destroyed during endoplasmic reticulum-associated degradation (ERAD). For example, chaperones are thought to solubilize aggregation-prone motifs, and some data suggest that these proteins are degraded at the ER. To better define how membrane proteins are destroyed, the ERAD of Ste6p(*), a 12 transmembrane protein, was reconstituted. We found that specific Hsp70/40s act before ubiquitination and facilitate Ste6p(*) association wi ...[more]