Erratum: Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone

Nature Communications 1: Article number: 79 (2010); Published: 21 September 2010; Updated: 31 January 2012.

The image in Figure 5d of this Article was inadvertently duplicated from panel e. The correct version of the figure appears below.

Figure 5: CNPY3–TLR9 interaction is dependent on gp96.
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(a) Expression of endogenous CNPY3 and gp96 by Raw264.7 after transduction with empty vector (EV), and one or two rounds of gp96 shRNA lentivector. β-Actin is shown as a loading control. (b) Lack of cleaved form of TLR9 (TLR9 m) in the absence of gp96 or CNPY3. Total lysates of wild-type (WT) Raw264.7, cells that were knocked down (KD) for gp96 (gp96 KD) or CNPY3 (CNPY3 KD) were untreated, or treated with Endo H or PNGase F, followed by IB for TLR9HA. (c) WT or gp96 Mut pre-B cells were immunoblotted for TLR9-HA, gp96, CNPY3-FLAG and β-actin. (d) IP of CNPY3 from WT or gp96 KO cells, followed by IB for indicated proteins. (e) IP of TLR9-HA from WT or gp96 KO cells, followed by IB for indicated proteins. ISO indicated IP with isotype control antibody. Two experiments were conducted with similar results.

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Correspondence to Zihai Li.

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The online version of the original article can be found at 10.1038/ncomms1070

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Liu, B., Yang, Y., Qiu, Z. et al. Erratum: Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone. Nat Commun 3, 653 (2012). https://doi.org/10.1038/ncomms1398

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