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Akt binds prohibitin 2 and relieves its repression of MyoD and muscle differentiation.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Sun, Luguo Liu, Lanying Yang, X. M. Wu, Zhenguo |
| Copyright Year | 2004 |
| Abstract | In a yeast two-hybrid screen using the full-length Akt as bait, we found that prohibitin 2 (PHB2) specifically interacts with Akt. The C terminus of Akt (amino acids 413-480) and a central region of PHB2 (amino acids 120-232) are responsible for their mutual interaction. PHB2 acts as a transcriptional repressor in cells. PHB2 interacts with both MyoD and MEF2, and represses both MyoD- and MEF2-dependent gene transcription. Furthermore, binding of PHB2 to both MyoD and MEF2 significantly decreases upon myogenic differentiation. When stably expressed in C2C12 myogenic cells, PHB2 inhibits myogenin induction and phenotypic muscle differentiation. PHB2 was found to specifically recruit histone deacetylase 1, which is probably responsible for its repressive activity. Co-expression of Akt can partially reduce PHB2 binding to MyoD and relieve the repressive effect of PHB2 on myogenic reporters, which could be one of the mechanisms underlying Akt-mediated MyoD activation and accelerated muscle differentiation. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://jcs.biologists.org/content/joces/early/2004/06/01/jcs.01142.full.pdf |
| Alternate Webpage(s) | http://jcs.biologists.org/content/joces/117/14/3021.full.pdf |
| Alternate Webpage(s) | http://jcs.biologists.org/content/117/14/3021.full.pdf |
| PubMed reference number | 15173318v1 |
| Volume Number | 117 |
| Part | 14 |
| Journal | Journal of cell science |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Amino Acids Cell Differentiation process Histone Deacetylase Histones MYOD1 gene MYOD1 wt Allele PHB gene PHB2 gene Proto-Oncogene Proteins c-akt Repression, Psychology SMRT protein Transcription Repressor/Corepressor Transcription, Genetic muscle cell differentiation |
| Content Type | Text |
| Resource Type | Article |
