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Phospho‐ablated Id2 is pro‐apoptotic in C2C12 myotubes
Author(s) -
Butler David Christopher,
Haramizu Satoshi,
Asano Shinichi,
Alway Stephen E.
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.2_supplement.147
Subject(s) - c2c12 , myogenesis , ectopic expression , phosphorylation , apoptosis , microbiology and biotechnology , regulator , myocyte , biology , serine , chemistry , biochemistry , gene
Inhibitor of differentiation protein‐2 (Id2) is a dominant negative helix‐loop‐helix protein, and a positive regulator of proliferation, in various cells. The N‐terminal region of Id2 contains a consensus cdk2 phosphorylation sequence SPVR located at serine 5, which has been shown to be involved with the induction of apoptosis in C2C12 myoblasts. Adeno‐associated viral vectors (AAV1) that expressed wild type Id2, phospho‐ablated Id2S5A, phospho‐mimicking Id2S5A, and green fluorescent protein (GFP) were used to determine if the phosphorylation of Id2 induces apoptosis in C2C12 myotubes. There was a significant increase in the caspase 9 and caspase 3 activities in C2C12 myotubes infected with phospho‐ablated Id2. These data suggest that the ectopic expression of unphosphorylated Id2S5A is pro‐apoptotic in C2C12 myotubes, and potentially working through the intrinsic pathway for apoptosis.