Department of Medicine, Department of Cell Biology, Montefiore-Einstein Center for Cardiovascular Research, Albert Einstein Cancer Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461 USA
Nothing is known about the regulation of NOP30. The regulation of ARC is complex. ARC protein abundance decreases rapidly and dramatically in response to hypoxia and oxidative stress (e.g. ischemia-reperfusion) (Ekhterae et al., 1999; Neuss et al., 2001; Nam et al., 2007). These decreases result from increased degradation of ARC protein via the ubiquitin-proteasomal pathway (Nam et al., 2007). The E3 ligase MDM2 may play a role in ARC degradation in this scenario (Foo et al., JBC, 2007), but this role is probably indirect (L. Wu and R. Kitsis, unpublished data). Decreases in ARC protein abundance in response to hypoxia appear to be regulated by p53 repression of nol3 transcription (Li et al., 2008). Apart from ARC protein abundance, the activity of ARC is also regulated post-translationally: dephosphorylation of threonine 149 decreases the anti-apoptotic activity of ARC (Tan et al., 2008).
NCBI: 8996 MIM: 605235 HGNC: 7869 Ensembl: ENSG00000140939
dbSNP: 8996 ClinVar: 8996 TCGA: ENSG00000140939 COSMIC: NOL3
Gloria Kung ; Wendy McKimpson ; Richard N Kitsis
NOL3 (nucleolar protein 3 (apoptosis repressor with CARD domain))
Atlas Genet Cytogenet Oncol Haematol. 2009-05-01
Online version: http://atlasgeneticsoncology.org/gene/41552/gene-explorer/favicon/apple-touch-icon.png