Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/96780
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dc.contributor.authorMisra, Ashishen
dc.contributor.authorGeorge, Bhawanaen
dc.contributor.authorRajmohan, Rajamuthiahen
dc.contributor.authorJain, Neerajen
dc.contributor.authorWong, Ming Hwaen
dc.contributor.authorKambadur, Ravien
dc.contributor.authorThanabalu, Thirumaranen
dc.date.accessioned2013-07-16T07:22:19Zen
dc.date.accessioned2019-12-06T19:35:02Z-
dc.date.available2013-07-16T07:22:19Zen
dc.date.available2019-12-06T19:35:02Z-
dc.date.copyright2012en
dc.date.issued2012en
dc.identifier.citationMisra, A., George, B., Rajmohan, R., Jain, N., Wong, M. H., Kambadur, R., et al. (2012). Insulin Receptor Substrate protein 53kDa (IRSp53) is a negative regulator of myogenic differentiation. The International Journal of Biochemistry & Cell Biology, 44(6), 928-941.en
dc.identifier.issn1357-2725en
dc.identifier.urihttps://hdl.handle.net/10356/96780-
dc.description.abstractFusion of mononucleated myoblasts to generate multinucleated myotubes is a critical step in skeletal muscle development. Filopodia, the actin cytoskeleton based membrane protrusions, have been observed early during myoblast fusion, indicating that they could play a direct role in myogenic differentiation. The control of filopodia formation in myoblasts remains poorly understood. Here we show that the expression of IRSp53 (Insulin Receptor Substrate protein 53 kDa), a known regulator of filopodia formation, is down-regulated during differentiation of both mouse primary myoblasts and a mouse myoblast cell line C2C12. Over-expression of IRSp53 in C2C12 cells led to induction of filopodia and decrease in cell adhesion, concomitantly with inhibition of myogenic differentiation. In contrast, knocking down the IRSp53 expression in C2C12 cells led to a small but significant increase in myotube development. The decreased cell adhesion of C2C12 cells over-expressing IRSp53 is correlated with a reduction in the number of vinculin patches in these cells. Mutations in the conserved IMD domain (IRSp53 and MIM (missing in metastasis) homology domain) or SH3 domain of IRSp53 abolished the ability of this protein to inhibit myogenic differentiation and reduce cell adhesion. Over-expression of the IMD domain alone was sufficient to decrease the cell–extracellular matrix adhesion and to inhibit myogenesis in a manner dependent on its function in membrane shaping. Based on our data, we propose that IRSp53 is a negative regulator of myogenic differentiation which correlates with the observed down regulation of IRSp53 expression during myoblast differentiation to myotubes.en
dc.language.isoenen
dc.relation.ispartofseriesThe international journal of biochemistry & cell biologyen
dc.rights© 2012 Elsevier Ltd.en
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleInsulin receptor substrate protein 53kDa (IRSp53) is a negative regulator of myogenic differentiationen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1016/j.biocel.2012.02.020en
item.grantfulltextnone-
item.fulltextNo Fulltext-
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