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Differential effects of PDCD4 depletion on protein synthesis in myoblast and myotubes.


ABSTRACT: BACKGROUND: Reduced muscle mass is a hallmark of metabolic diseases like diabetes and cancer. The mammalian (mechanistic) target of rapamycin complex 1/S6 kinase 1 (mTORC1/S6K1) pathway is critical to the regulation of muscle protein synthesis and mass but its mechanism of action is not completely understood. RESULTS: Using L6 myotubes, we characterized the regulation of programmed cell death 4 (PDCD4), a recently described substrate of S6K1. The abundance, but not Ser67 phosphorylation, of PDCD4 was sensitive to amino acid and serum deprivation: values in starved cells were 4.5X of control (P?

SUBMITTER: Kakade D 

PROVIDER: S-EPMC3893489 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Differential effects of PDCD4 depletion on protein synthesis in myoblast and myotubes.

Kakade Dhanshri D   Islam Nushaba N   Maeda Naomi N   Adegoke Olasunkanmi A J OA  

BMC cell biology 20140109


<h4>Background</h4>Reduced muscle mass is a hallmark of metabolic diseases like diabetes and cancer. The mammalian (mechanistic) target of rapamycin complex 1/S6 kinase 1 (mTORC1/S6K1) pathway is critical to the regulation of muscle protein synthesis and mass but its mechanism of action is not completely understood.<h4>Results</h4>Using L6 myotubes, we characterized the regulation of programmed cell death 4 (PDCD4), a recently described substrate of S6K1. The abundance, but not Ser67 phosphoryla  ...[more]

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