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Corrigendum
Open Access | 
10.1172/JCI162883
Numb and Numblike regulate sarcomere assembly and maintenance
Baolei Wang, Min Yang, and Shujuan Li
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Published July 15, 2022 - More info
J Clin Invest. 2022;132(14):e162883. https://doi.org/10.1172/JCI162883.
© 2022 Numb et al. This work is licensed under the Creative Commons Attribution 4.0 International License. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
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Abstract
A sarcomere is the contractile unit of the myofibril in striated muscles such as cardiac and skeletal muscles. The assembly of sarcomeres depends on multiple molecules that serve as raw materials and participate in the assembly process. However, the mechanism of this critical assembly process remains largely unknown. Here, we found that the cell fate determinant Numb and its homolog Numblike regulated sarcomere assembly and maintenance in striated muscles. We discovered that Numb and Numblike are sarcomeric molecules that were gradually confined to the Z-disc during striated muscle development. Conditional knockout of Numb and Numblike severely compromised sarcomere assembly and its integrity and thus caused organelle dysfunction. Notably, we identified that Numb and Numblike served as sarcomeric α-Actin–binding proteins (ABPs) and shared a conserved domain that can bind to the barbed end of sarcomeric α-Actin. In vitro fluorometric α-Actin polymerization assay showed that Numb and Numblike also played a role in the sarcomeric α-Actin polymerization process. Last, we demonstrate that Numb and Numblike regulate sarcomeric α-Actinin–dependent (ACTN-dependent) Z-disc consolidation in the sarcomere assembly and maintenance. In summary, our studies show that Numb and its homolog Numblike regulate sarcomere assembly and maintenance in striated muscles, and demonstrate a molecular mechanism by which Numb/Numblike, sarcomeric α-Actin, and ACTN cooperate to control thin filament formation and Z-disc consolidation.
Authors
Baolei Wang, Min Yang, Shujuan Li
Original citation: J Clin Invest. 2022;132(3):e139420. https://doi.org/10.1172/JCI139420
Citation for this corrigendum: J Clin Invest. 2022;132(14):e162883. https://doi.org/10.1172/JCI162883
Following the publication of this article, the authors noted several errors that require correction. All observations ascribed to day p60 were actually made at p60.5. Furthermore, in Figure 3E, construct 6 was inaccurately depicted. The correct panel is shown below.
The description of Figure 3E in the Results section has also been corrected, as below:
The results indicate that Numb (173–322 aa) and Numblike (1–366 aa) were the dominant residue sequences that interacted with ACTC1 and that Numblike (1–205 aa) and Numblike (367–604 aa) had negligible functional interactions with ACTC1 (Figure 3F). After blasting the Numb (173–322 aa) and Numblike (1– 366 aa) amino acid sequences in the NCBI database, we found that these 2 sequences were highly conserved, indicating the potentially critical role of these conservative domains in α-Actin binding (Supplemental Figure 9A).
In the Discussion section, a corrected sentence has been included, as below:
Since the expression of MLC-2v is restricted within the ventricular chamber throughout mouse embryonic development, this mouse line serves as a great platform to study how Numb and Numblike affect sarcomere assembly in ventricular CMs at the early stage (19, 26).
The text and Figure 3E have been updated in the HTML version and PDF with the correct information.
The authors regret the errors.
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ISSN: 0021-9738 (print), 1558-8238 (online)