| Literature DB >> 24799716 |
Zhe Chen1, William Holland2, John M Shelton3, Aktar Ali4, Xiaoming Zhan1, Sungyong Won1, Wataru Tomisato1, Chen Liu5, Xiaohong Li1, Eva Marie Y Moresco1, Bruce Beutler6.
Abstract
Sterile alpha motif domain containing protein 4 (Samd4) is an RNA binding protein that mediates translational repression. We identified a Samd4 missense mutation, designated supermodel, that caused leanness and kyphosis associated with myopathy and adipocyte defects in C57BL/6J mice. The supermodel mutation protected homozygous mice from high fat diet-induced obesity, likely by promoting enhanced energy expenditure through uncoupled mitochondrial respiration. Glucose tolerance was impaired due to diminished insulin release in homozygous mutant mice. The defects of metabolism in supermodel mice may be explained by dysregulated mechanistic target of rapamycin complex 1 (mTORC1) signaling, evidenced by hypophosphorylation of 4E-BP1 and S6 in muscle and adipose tissues of homozygous mice. Samd4 may interface with mTORC1 signaling through an interaction with 14-3-3 proteins and with Akt, which phosphorylates Samd4 in vitro.Entities:
Keywords: Akt/PKB; N-ethyl-N-nitrosourea
Mesh:
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Year: 2014 PMID: 24799716 PMCID: PMC4034201 DOI: 10.1073/pnas.1406511111
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205