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. 2014 Nov 24;207(4):569. doi: 10.1083/jcb.20120200511112014c

ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load

Joseph E Chambers, Kseniya Petrova, Giulia Tomba, Michele Vendruscolo, David Ron
PMCID: PMC4242834

Vol. 198 No. 3, August 6, 2012. Pages 371–385.

The authors noted an error in the title of the legend for Fig. 2. A corrected version of the legend is appended below.

Figure 2.

Figure 2.

ADP-ribosylated BiP is enriched in low–molecular weight fractions of the ER extract. (A) Coomassie-stained SDS-PAGE of pancreatic microsomal proteins from fasted and fed mice resolved by gel filtration. BiP is distributed bimodally between a high–molecular weight peak containing the cochaperone ORP150 and GRP94 and lower–molecular weight peak. A representative experiment reproduced three times is shown. Abs., absorbance; mAU, milli–absorbance unit. (B) BiP immunoblot of IEF gels of the input (GF input) and fractions 9 and 14 of the fasted and 1-h refed samples above. The ratio of ADP ribosylated to total BiP in each lane is indicated (R). Black lines indicate that intervening lanes have been spliced out.

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