Correction: Corrigendum: The Phosphorylation Profile of Myosin Binding Protein-C Slow is Dynamically Regulated in Slow-Twitch Muscles in Health and Disease

Abstract

This Article contains errors in Figure 2, where the blots for (−) GST-sMyBP-C NH 2 aa1-285 , (+) GST-fMyBP-C NH 2 aa1-249 , (−) GST-fMyBP-C NH 2 aa1-249 , (+) GST-protein and (−) GST-protein (the right half of the panel) were duplicated between all panels. Additionally, blots for (+) GST-sMyBP-C NH 2 Δ 21-59 aa1-285 in panel 2c and (+) GST-sMyBP-C NH 2 aa1-285 in panel 2e were duplicated. The authors re-scanned the images for the blots presented in this figure. Data in panel 2a, samples (+) GST-sMyBP-C NH 2 Δ 21-59 aa1-285 , (+) GST-sMyBP-C NH 2 Δ 34-59 aa1-285 , (+) GST-sMyBP-C NH 2 aa1-285 , (+) GST-fMyBP-C NH 2 aa1-249, panel 2b, samples (+) GST-sMyBP-C NH 2 Δ 21-59 aa1-285 , (+) GST-sMyBP-C NH 2 Δ 34-59 aa1-285 , and (+) GST-sMyBP-C NH 2 aa1-285 , and panel 2d sample (+) GST-sMyBP-C NH 2 Δ 34-59 aa1-285 remain unchanged. All other images were replaced with re-scanned blots. All samples in the corrected figure are shown with the wider field of view. The correct Figure 2 appears below as Figure 1 and the Supplementary Information file has now been replaced. In the revised version of the Supplement the unprocessed images of full-length blots for all blots presented in Figure 2 are now included as Supplementary Figures 2-6.

Fast and slow skeletal myosin binding protein-C and aging

“…Our results, investigating age-associated alterations in phosphorylation levels in the sMyBP-C paralog and in the fMyBP-C, reveal no change in phosphorylation levels in the fast TA muscles from adult and old mice. Our data, reporting no change in sMyBP-C phosphorylation with age, aligns well with the reported no change in phosphorylation levels of sMyBP-C in the fast FDB muscles with age [ 10 , 20 ] and expands our knowledge of the fMyBP-C paralog. The overall interpretation of these findings suggests that both MyBP-C paralogs are constitutively phosphorylated at basal levels and it seems these levels are maintained with aging in these two fast muscles investigated to date.…”

“…With aging, there is evidence that changes in the phosphorylation status of specific residues in cMyBP-C may be a major contributor to the age-related loss of diastolic function in murine hearts [19]. Although the MyBP-C paralogs have yet to be fully described in aging skeletal muscles, there is differential phosphorylation of specific residues in the sMyBP-C paralog within the slow soleus and the fast flexor digitorum brevis muscles early in the lifespan (between the ages of 2 and 14 months) from WT mice and from mice with dystrophy (mdx mouse model) providing sufficient rationale for further investigation of this sarcomeric protein and its paralogs as potential factors contributing to the complex nature of sarcopenia [10,20]. Skeletal and heart muscles are also rich in mitochondria and have high metabolic demands, which provide microenvironments whereby the sarcomeric proteins are highly susceptible to oxidative damage [3,21,22].…”