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Correction

Correction for Vosler et al., Ischemia-induced calpain activation causes eukaryotic (translation) initiation factor 4G1 (eIF4GI) degradation, protein synthesis inhibition, and neuronal death

PNAS December 3, 2013 110 (49) 19968; https://doi.org/10.1073/pnas.1320015110
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NEUROSCIENCE Correction for “Ischemia-induced calpain activation causes eukaryotic (translation) initiation factor 4G1 (eIF4GI) degradation, protein synthesis inhibition, and neuronal death,” by Peter S. Vosler, Yanqin Gao, Christopher S. Brennan, Akiko Yanagiya, Yu Gan, Guodong Cao, Feng Zhang, Simon J. Morley, Nahum Sonenberg, Michael V. L. Bennett, and Jun Chen, which appeared in issue 44, November 1, 2011, of Proc Natl Acad Sci USA (108:18102–18107; first published October 17, 2011; 10.1073/pnas.1112635108).

The authors note that Fig. 3 appeared incorrectly. In panel 3E, the wrong image for the β-actin loading control was used for the Western blot. The corrected figure and its legend appear below. This error does not affect the conclusions of the article.

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Fig. 3.

Neuroprotection by eIF4G1 following ischemia is at least partially protein synthesis dependent. (A) Immunostaining for the HA tag was performed to assess transfection efficacy of lentiviral-mediated overexpression of HA-eIF4G1, and neuronal colocalization was demonstrated by costaining for MAP2. (B) Levels of initiation factors in primary neurons overexpressing HA-eIF4G1 (4G) compared with those in neurons expressing GFP are shown by Western blot. (C and D) Control (GFP-transfected) neurons and 4G-transfected neurons were untreated or exposed to 50 μM CHX for 24 h or subjected to 1 h OGD and 24 h reperfusion without or with 50 μMCHX. After 24 h, treated neurons were assessed for protein synthesis (cpm per microgram protein) (C) and viability (D). Both protein synthesis and survival were increased by 4G overexpression. (E) Western blot analysis showing the effect of GFP- or eIF4G1-transfection on the expression of regulatory translation initiation factors by neurons without OGD or subjected to 1 h OGD at 0, 2, and 24 h reperfusion. Specifically, P-eIF2α was transiently increased at 0 and 2 h as in Fig. 1F, and eIF4G1 was decreased at 24 h in control neurons. Bars represent mean ± SD of n = 3–4 independent experiments. *P < 0.05, **P < 0.01, and ***P < 0.001 compared with control and where indicated, ##P < 0.01 compared with control, GFP-transfected, CHX-treated neurons.

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Correction for Vosler et al., Ischemia-induced calpain activation causes eukaryotic (translation) initiation factor 4G1 (eIF4GI) degradation, protein synthesis inhibition, and neuronal death
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Correction for Vosler et al., Ischemia-induced calpain activation causes eukaryotic (translation) initiation factor 4G1 (eIF4GI) degradation, protein synthesis inhibition, and neuronal death
Proceedings of the National Academy of Sciences Dec 2013, 110 (49) 19968; DOI: 10.1073/pnas.1320015110

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Correction for Vosler et al., Ischemia-induced calpain activation causes eukaryotic (translation) initiation factor 4G1 (eIF4GI) degradation, protein synthesis inhibition, and neuronal death
Proceedings of the National Academy of Sciences Dec 2013, 110 (49) 19968; DOI: 10.1073/pnas.1320015110
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