Injury-Induced HDAC5 Nuclear Export Is Essential for Axon Regeneration
Author(s) -
Yongcheol Cho,
Roman Sloutsky,
Kristen M. Naegle,
Valeria Cavalli
Publication year - 2015
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2015.04.019
Subject(s) - serine , biology , alanine , histone deacetylase 5 , microbiology and biotechnology , mutant , aspartic acid , histone deacetylase , biochemistry , histone , amino acid , phosphorylation , gene
(Cell 155, 894–908; November 7, 2013) After the publication of this article, we noticed an error in the text describing the generation of cytosolic-trapped HDAC5 (GFPHDAC5cyto) in both the Results and Extended Experimental Procedures sections. The original text mistakenly referred to mutation of serine residues 259 and 498 to aspartic acid, generating a mostly cytoplasmic HDAC5 (GFP-HDAC5tcyto) mutant. This sentence omitted that, in addition, serine residue 280 was mutated to alanine. Indeed, the sequential mutagenesis process of the three point mutations was first serine 280 to alanine, second serine 259 to aspartic acid, and third serine 498 to aspartic acid. Hence, the accurate description is that mutation of serine residues 259 and 498 to aspartic acid and serine residue 280 to alanine generated mostly cytoplasmic HDAC5 (GFP-HDAC5tcyto) mutant. This error in the description of the HDAC5cyto construct, which was used in Figures 5E and S2A, does not affect the interpretation of the data, the results in the paper, or the overall conclusion of the study.We apologize for any confusion that this error may have caused.
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