A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation Bader, M., Benjamin, S., Wapinski, O.L., Smith, D.M., Goldberg, A.L., Steller, H. (2011). A conserved f box regulatory complex controls proteasome activity in Drosophila.  Cell 145(3): 371--382. (Export to RIS)
FlyBase ID FBrf0213568
Publication Type Research paper
PubMed ID 21529711
PubMed Abstract The ubiquitin-proteasome system catalyzes the degradation of intracellular proteins. Although ubiquitination of proteins determines their stabilities, there is growing evidence that proteasome function is also regulated. We report the functional characterization of a conserved proteasomal regulatory complex. We identified DmPI31 as a binding partner of the F box protein Nutcracker, a component of an SCF ubiquitin ligase (E3) required for caspase activation during sperm differentiation in Drosophila. DmPI31 binds Nutcracker via a conserved mechanism that is also used by mammalian FBXO7 and PI31. Nutcracker promotes DmPI31 stability, which is necessary for caspase activation, proteasome function, and sperm differentiation. DmPI31 can activate 26S proteasomes in vitro, and increasing DmPI31 levels suppresses defects caused by diminished proteasome activity in vivo. Furthermore, loss of DmPI31 function causes lethality, cell-cycle abnormalities, and defects in protein degradation, demonstrating that DmPI31 is physiologically required for normal proteasome activity.
DOI 10.1016/j.cell.2011.03.021
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Language of Publication English
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Publication Type Journal
Abbreviation Cell
Title Cell
Publication Year 1974-
ISBN/ISSN 0092-8674
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