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TRIM72 negatively regulates myogenesis via targeting insulin receptor substrate-1.

Authors
Lee, CS; Yi, JS; Jung, SY; Kim, BW; Lee, NR; Choo, HJ; Jang, SY; Han, J; Chi, SG; Park, M; Lee, JH; Ko, YG
Citation
Cell death and differentiation, 17(8):1254-1265, 2010
Journal Title
Cell death and differentiation
ISSN
1350-90471476-5403
Abstract
Lipid rafts have been known to be platforms to initiate cellular signal transduction of insulin-like growth factor (IGF) inducing skeletal muscle differentiation and hypertrophy. Here, tripartite motif 72 (TRIM72), with a really interesting new gene (RING)-finger domain, a B-box, two coiled-coil domains, and a SPRY (SPla and RYanodine receptor) domain, was revealed to be predominantly expressed in the sarcolemma lipid rafts of skeletal and cardiac muscles. Adenoviral TRIM72 overexpression prevented but RNAi-mediated TRIM72 silencing enhanced C2C12 myogenesis by modulating the IGF-induced insulin receptor substrate-1 (IRS-1) activation through the molecular association of TRIM72 with IRS-1. Furthermore, myogenic activity was highly enhanced with increased IGF-induced Akt activation in the satellite cells of TRIM72(-/-) mice, compared to those of TRIM72+/+ mice. Because TRIM72 promoter analysis shows that two proximal E-boxes in TRIM72 promoter were essential for MyoD- and Akt-dependent TRIM72 transcription, we can conclude that TRIM72 is a novel antagonist of IRS-1, and is essential as a negative regulator of IGF-induced muscle differentiation.
MeSH terms
AnimalsCarrier Proteins/antagonists & inhibitorsCarrier Proteins/geneticsCarrier Proteins/metabolism*Cell DifferentiationCell LineFemaleInsulin Receptor Substrate Proteins/metabolism*MaleMembrane Microdomains/metabolismMiceMuscle Development*Muscle, Skeletal/physiology*Proto-Oncogene Proteins c-akt/metabolismRNA InterferenceRNA, Small Interfering/metabolismSatellite Cells, Skeletal Muscle/cytologySatellite Cells, Skeletal Muscle/metabolismSignal Transduction
DOI
10.1038/cdd.2010.1
PMID
20139895
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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