ArticleCell motility and the cytoskeleton2008
Role of nonmuscle myosin IIB and N-RAP in cell spreading and myofibril assembly in primary mouse cardiomyocytes.
Article in Cell motility and the cytoskeleton, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Transcriptomic profiling of cardiac development in Bama Xiang pigs across key developmental stages.Zoological research · 2025Article
- A novel loss-of-function mutation in NRAP is associated with left ventricular non-compaction cardiomyopathy.Frontiers in cardiovascular medicine · 2023Article
- An adapted particle swarm optimization algorithm as a model for exploring premyofibril formation.AIP advances · 2020Article
- Nonmuscle myosin II in cardiac and skeletal muscle cells.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Exome sequencing identifies variants in two genes encoding the LIM-proteins NRAP and FHL1 in an Italian patient with BAG3 myofibrillar myopathy.Journal of muscle research and cell motility · 2016Article
- Heavy and light roles: myosin in the morphogenesis of the heart.Cellular and molecular life sciences : CMLS · 2013Review
- Identification of an FHL1 protein complex containing gamma-actin and non-muscle myosin IIB by analysis of protein-protein interactions.PloS one · 2013Article
- Scaffolds and chaperones in myofibril assembly: putting the striations in striated muscle.Biophysical reviews · 2011Article
- Myofibril assembly visualized by imaging N-RAP, alpha-actinin, and actin in living cardiomyocytes.Experimental cell research · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We investigated the role of nonmuscle myosin heavy chain (NMHC) IIB in cultured embryonic mouse cardiomyocytes by specific knockdown using RNA interference. NMHC IIB protein levels decreased 90% compared with mock-transfected cells by 3 days post transfection. NMHC IIB knockdown resulted in a slow decrease in N-RAP protein levels over 6 days with no change in N-RAP transcript levels. N-RAP is a scaffold for alpha-actinin and actin assembly during myofibrillogenesis, and we quantitated myofibril accumulation by morphometric analysis of alpha-actinin organization. Between 3 and 6 days, NMHC IIB knockdown was accompanied by the abolishment of cardiomyocyte spreading. During this period the rate of myofibril accumulation steadily decreased, correlating with the slowly decreasing levels of N-RAP. Between 6 and 8 days NMHC IIB and N-RAP protein levels recovered, and cardiomyocyte spreading and myofibril accumulation resumed. Inhibition of proteasome function using MG132 led to accumulation of excess N-RAP, and the secondary decrease in N-RAP that otherwise accompanied NMHC IIB knockdown was abolished. The results show that NMHC IIB knockdown led to decreased N-RAP levels through proteasome-mediated degradation. Furthermore, these proteins have distinct functional roles, with NMHC IIB playing a role in cardiomyocyte spreading and N-RAP functioning in myofibril assembly.
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