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. Author manuscript; available in PMC: 2015 Sep 9.
Published in final edited form as: IET Syst Biol. 2012 Apr;6(2):54–63. doi: 10.1049/iet-syb.2011.0006

Fig. 1. Molecular chaperone BiP/Kar2 is required for efficient protein translocation into the ER lumen, protein folding and maturation and ERAD.

Fig. 1

Interactions with selective co-chaperones include membrane protein Sec63 and freely diffusing Scj1 and Jem1. Intrinsic rates of peptide release are low; thus following ATP hydrolysis, nucleotide exchange is facilitated by Sil1 or Lhs1. In this illustration, Sec61 is a member of the ER membrane pore complex responsible for translocation and possibly the transport of aberrant proteins by ERAD