The stability of eukaryotic initiation factor 2-associated glycoprotein, p67, increases during skeletal muscle differentiation and that inhibits the phosphorylation of extracellular signal-regulated kinases 1 and 2 |
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Authors: | Datta Bansidhar Datta Rekha Majumdar Avijit Ghosh Arnab |
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Affiliation: | Department of Chemistry, Kent State University, Kent, OH 44242, United States. bdatta@kent.edu |
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Abstract: | Eukaryotic initiation factor 2-associated glycoprotein, p67, protects eIF2 from phosphorylation by its kinases. To understand the roles of p67 during skeletal muscle differentiation of mouse C2C12 myoblasts, we measured the level of p67 during myotube formation. We noticed that the level of p67 increases during myoblast differentiation and this increased level is controlled at the translational stage. The stability of p67 in the myotubes is due to its low turnover rate. The phosphorylation of the extracellular signal-regulated kinases (ERKs 1 and 2) is high in growth-factor-mediated cycling of C2C12 myoblasts and this phosphorylation decreases at 96 h when these myoblasts are grown in differentiation medium. At this time of differentiation, the level of p67 is higher compared to 0 h of differentiation. p67 binds to ERK2 and inhibits its activity in vitro. Taken together, these results suggest that the stability of p67 increases during myotube formation while inhibiting the phosphorylation of ERKs 1 and 2. |
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Keywords: | p67, eukaryotic initiation factor 2-associated 67-kDa glycoprotein eIF2α, α-subunit of eukaryotic initiation factor 2 (eIF2) eIF2α(P), phosphorylated form of eIF2α EGFP, enhanced green fluorescent protein ERK1 and ERK2, extracellular signal-regulated kinases 1 and 2 p-ERK1/2, phosphorylated form of ERK1/2 IPs, immunoprecipitates MBP, myelin basic protein |
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