Intracellular Localization, and Protein Synthesis of Myod and Id1 during Muscle Differentiation
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چکیده
UBIQUITIN-PROTEASOME-MEDIATED DEGRADATION, INTRACELLULAR LOCALIZATION, AND PROTEIN SYNTHESIS OF MYOD AND ID1 DURING MUSCLE DIFFERENTIATION Liping Sun‡, Julie S. Trausch-Azar‡, Aaron Ciechanover§ and Alan L. Schwartz‡ From the ‡ Edward Malincrodt Department of Pediatrics and Molecular biology and Pharmacology, Washington University School of Medicine and St.Louis Children’s Hospital, St.Louis, Missouri 63110 and the § Department of Biochemistry and Rappaport Institute for Research in Medical Sciences, Faculty of Medicine, Technion-Israel Institute for Technology, Haifa 31096, Israel Running Title: MyoD and Id1 degradation in muscle differentiation Address correspondence to: Alan L. Schwartz, Ph.D, M.D., Department of Pediatrics, Washington University School of Medicine, 660 S. Euclid Avenue, C.B. 8116, St. Louis, MO 63110, Telephone: 314-454-6005; Fax: 314-454-0537; E-mail: [email protected]
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Ubiquitin-proteasome-mediated degradation, intracellular localization, and protein synthesis of MyoD and Id1 during muscle differentiation.
Mammalian skeletal myogenesis results in the differentiation of myoblasts to mature syncytial myotubes, a process regulated by an intricate genetic network of at least three protein families: muscle regulatory factors, E proteins, and Id proteins. MyoD, a key muscle regulatory factor, and its negative regulator Id1 have both been shown to be degraded by the ubiquitin-proteasome system. Using C2...
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