Corrigendum to “The human phenotype of ornithine decarboxylase superactivity: a new syndrome”
Year: 2019
Type: erratum
Abstract: Am J Med Genet A. 2018 Dec;176(12):2545-2547. In the version of this article originally published, it was incorrectly stated that the first patient with ornithine decarboxylase (ODC) superactivity was reported in the December 2019 issue of American Journal of Medical Genetics part A, while the patient was originally reported in the December 2018 issue. In addition, it was stated that antizymes inhibit ODC and target it for proteasomal degradation by binding to its C-terminus. Although it is factually correct that antizymes inhibit ODC, and that the C-terminus plays a role in the degradation of ODC, the binding site of antizyme does not reside in the C-terminus. The putative site of the antizyme-binding element lies between residues 117–140 of the 461-amino acid protein (Almrud et al., 2000), while the C-terminus (cODC) lies between residues 425–461 (Takeuchi, Chen, Hoyt, & Coffino, 2008). Although antizymes bind ODC and enhance its degradation, the C-terminus of ODC represents an autonomous element that mediates degradation of ODC even in the absence of antizymes (Takeuchi et al., 2008). In fact, antizymes likely enhance degradation of the ODC-antizyme heterodimer at least in part by inducing a conformational change that exposes cODC to the proteasome (Li & Coffino, 1993). The now accessible cODC mediates two functions that are relevant to the ubiquitin-independent degradation of ODC: first, the cysteine at residue 441 serves to tether ODC to the proteasome, while the more distal residues provide an unstructured region essential for proteasomal entry (Erales & Coffino, 2014; Takeuchi et al., 2008). These two errors have now been corrected in the online version of the article. We apologize for this oversight.
DOI: 10.1002/ajmg.a.61064
Author: Carlos R. Ferreira
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2911484181