ArticleThe Biochemical journal2004
Myristoylated alanine-rich C kinase substrate (MARCKS) is involved in myoblast fusion through its regulation by protein kinase Calpha and calpain proteolytic cleavage.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Advancements in Omics and Breakthrough Gene Therapies: A Glimpse into the Future of Peripheral Artery Disease.Annals of vascular surgery · 2024Review
- Poor maternal diet during gestation alters offspring muscle proteome in sheep.Journal of animal science · 2022Article
- Myristoylated alanine-rich C kinase substrate-like protein-1 regulates epithelial sodium channel activity in renal distal convoluted tubule cells.American journal of physiology. Cell physiology · 2020Article
- Calpainopathy: Description of a Novel Mutation and Clinical Presentation with Early Severe Contractures.Genes · 2020Article
- Calpain-1 and Calpain-2 in the Brain: Dr. Jekill and Mr Hyde?Current neuropharmacology · 2019Review
- The MARCKS protein amount is differently regulated by calpain during toxic effects of methylmercury between SH-SY5Y and EA.hy926 cells.The Journal of veterinary medical science · 2017Article
- ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins.American journal of physiology. Cell physiology · 2017Article
- MARCKS is involved in methylmercury-induced decrease in cell viability and nitric oxide production in EA.hy926 cells.The Journal of veterinary medical science · 2016Article
- Calpain-10 Activity Underlies Angiotensin II-Induced Aldosterone Production in an Adrenal Glomerulosa Cell Model.Endocrinology · 2015Article
- In Vitro Neutrophil Migration Requires Protein Kinase C-Delta (δ-PKC)-Mediated Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Phosphorylation.Inflammation · 2015Article
- Targeting calpain in synaptic plasticity.Expert opinion on therapeutic targets · 2013Review
- Fibroblast Migration Is Regulated by Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Protein.PloS one · 2013Article
- Calpain and MARCKS protein regulation of airway mucin secretion.Pulmonary pharmacology & therapeutics · 2012Article
- Transcriptional profile of GTP-mediated differentiation of C2C12 skeletal muscle cells.Purinergic signalling · 2012Article
- Lipocalin-type prostaglandin D2 synthase protein regulates glial cell migration and morphology through myristoylated alanine-rich C-kinase substrate: prostaglandin D2-independent effects.The Journal of biological chemistry · 2012Article
- MARCKS silencing differentially affects human vascular smooth muscle and endothelial cell phenotypes to inhibit neointimal hyperplasia in saphenous vein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009Article
- LongSAGE analysis of skeletal muscle at three prenatal stages in Tongcheng and Landrace pigs.Genome biology · 2007Article
- C6ORF32 is upregulated during muscle cell differentiation and induces the formation of cellular filopodia.Developmental biology · 2007Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MARCKS (myristoylated alanine-rich C kinase substrate) is a major cytoskeletal protein substrate of PKC (protein kinase C) whose cellular functions are still unclear. However numerous studies have implicated MARCKS in the stabilization of cytoskeletal structures during cell differentiation. The present study was performed to investigate the potential role of Ca(2+)-dependent proteinases (calpains) during myogenesis via proteolysis of MARCKS. It was first demonstrated that MARCKS is a calpain substrate in vitro. Then, the subcellular expression of MARCKS was examined during the myogenesis process. Under such conditions, there was a significant decrease in MARCKS expression associated with the appearance of a 55 kDa proteolytic fragment at the time of intense fusion. The addition of calpastatin peptide, a specific calpain inhibitor, induced a significant decrease in the appearance of this fragment. Interestingly, MARCKS proteolysis was dependent of its phosphorylation by the conventional PKCalpha. Finally, ectopic expression of MARCKS significantly decreased the myoblast fusion process, while reduced expression of the protein with antisense oligonucleotides increased the fusion. Altogether, these data demonstrate that MARCKS proteolysis is necessary for the fusion of myoblasts and that cleavage of the protein by calpains is involved in this regulation.
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