Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis
The striated muscle-specific mitsugumin 53 (MG53) is a novel E3 ligase that induces the ubiquitination of insulin receptor substrate 1 (IRS-1) during skeletal myogenesis, negatively regulating insulin-like growth factor and insulin signaling. Here we show that focal adhesion kinase (FAK) is the seco...
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2022
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| Thư viện lưu trữ: | Thư viện Trường Đại học Đà Lạt |
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oai:scholar.dlu.edu.vn:123456789-1570 |
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Thư viện Trường Đại học Đà Lạt |
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English |
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Focal Adhesion Kinase, Myogenesis, Skeletal Muscle, Ubiquitin-conjugating Enzyme (Ubc), Ubiquitin-dependent Protease |
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Focal Adhesion Kinase, Myogenesis, Skeletal Muscle, Ubiquitin-conjugating Enzyme (Ubc), Ubiquitin-dependent Protease Nguyễn, Thị Huỳnh Nga Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis |
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The striated muscle-specific mitsugumin 53 (MG53) is a novel E3 ligase that induces the ubiquitination of insulin receptor substrate 1 (IRS-1) during skeletal myogenesis, negatively regulating insulin-like growth factor and insulin signaling. Here we show that focal adhesion kinase (FAK) is the second target of MG53 during skeletal myogenesis. The FAK protein level gradually decreased, whereas its mRNA level was constant during myogenesis in C2C12 cells and MyoD-overexpressing mouse embryonic fibroblasts. The FAK protein was associated with the E2 enzyme UBE2H and the E3 enzyme MG53 in endogenous and exogenous immunoprecipitation experiments. FAK ubiquitination and degradation was induced by MG53 overexpression in myoblasts but abolished by MG53 or UBE2H knockdown in myotubes. Because RING-disrupted MG53 mutants (C14A and ΔR) did not induce FAK ubiquitination and degradation, the RING domain was determined to be required for MG53-induced FAK ubiquitination. Taken together, these data indicate that MG53 induces FAK ubiquitination with the aid of UBE2H during skeletal myogenesis. |
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Journal article |
| author |
Nguyễn, Thị Huỳnh Nga |
| author_facet |
Nguyễn, Thị Huỳnh Nga |
| author_sort |
Nguyễn, Thị Huỳnh Nga |
| title |
Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis |
| title_short |
Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis |
| title_full |
Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis |
| title_fullStr |
Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis |
| title_full_unstemmed |
Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis |
| title_sort |
mitsugumin 53 (mg53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis |
| publishDate |
2022 |
| url |
http://scholar.dlu.edu.vn/handle/123456789/1570 |
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1768306088815362048 |
| spelling |
oai:scholar.dlu.edu.vn:123456789-15702022-11-09T06:42:20Z Mitsugumin 53 (MG53) ligase ubiquitinates focal adhesion kinase during skeletal myogenesis Nguyễn, Thị Huỳnh Nga Focal Adhesion Kinase, Myogenesis, Skeletal Muscle, Ubiquitin-conjugating Enzyme (Ubc), Ubiquitin-dependent Protease The striated muscle-specific mitsugumin 53 (MG53) is a novel E3 ligase that induces the ubiquitination of insulin receptor substrate 1 (IRS-1) during skeletal myogenesis, negatively regulating insulin-like growth factor and insulin signaling. Here we show that focal adhesion kinase (FAK) is the second target of MG53 during skeletal myogenesis. The FAK protein level gradually decreased, whereas its mRNA level was constant during myogenesis in C2C12 cells and MyoD-overexpressing mouse embryonic fibroblasts. The FAK protein was associated with the E2 enzyme UBE2H and the E3 enzyme MG53 in endogenous and exogenous immunoprecipitation experiments. FAK ubiquitination and degradation was induced by MG53 overexpression in myoblasts but abolished by MG53 or UBE2H knockdown in myotubes. Because RING-disrupted MG53 mutants (C14A and ΔR) did not induce FAK ubiquitination and degradation, the RING domain was determined to be required for MG53-induced FAK ubiquitination. Taken together, these data indicate that MG53 induces FAK ubiquitination with the aid of UBE2H during skeletal myogenesis. 289 6 3209–3216 2022-11-09T02:47:29Z 2022-11-09T02:47:29Z 2014 Journal article Bài báo đăng trên tạp chí thuộc ISI, bao gồm book chapter http://scholar.dlu.edu.vn/handle/123456789/1570 10.1074/jbc.M113.525154 en JOURNAL OF BIOLOGICAL CHEMISTRY 0021-9258 1. Bisht, B., and Dey, C. S. (2008) Focal adhesion kinase contributes to insulin- induced actin reorganization into a mesh harboring glucose transporter-4 in insulin resistant skeletal muscle cells. BMC Cell Biol. 9, 48 2. Flück, M., Ziemiecki, A., Billeter, R., and Müntener, M. 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