| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1950890 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2011 | 8 Pages |
Mutations in cereblon (CRBN), a substrate binding component of the E3 ubiquitin ligase complex, cause a form of mental retardation in humans. However, the cellular proteins that interact with CRBN remain largely unknown. Here, we report that CRBN directly interacts with the α1 subunit of AMP-activated protein kinase (AMPK α1) and inhibits the activation of AMPK activation. The ectopic expression of CRBN reduces phosphorylation of AMPK α1 and, thus, inhibits the enzyme in a nutrient-independent manner. Moreover, AMPK α1 can be potently activated by suppressing endogenous CRBN using CRBN-specific small hairpin RNAs. Thus, CRBN may act as a negative modulator of the AMPK signaling pathway in vivo.
Research highlights►Cereblon (CRBN) directly interacts with the AMP-activated protein kinase (AMPK) α1. ►Expression of CRBN reduces the phosphorylation of AMPK α1. ►AMPK α1 can be potently activated by suppressing endogenous CRBN.
