ArticleGene expression2005
Casein kinase II phosphorylation regulates alphaNAC subcellular localization and transcriptional coactivating activity.
Article in Gene expression, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Dephosphorylation of the transcriptional cofactor NACA by the PP1A phosphatase enhances cJUN transcriptional activity and osteoblast differentiation.The Journal of biological chemistry · 2019Article
- Combinatorial control of ATF4-dependent gene transcription in osteoblasts.Annals of the New York Academy of Sciences · 2011Review
- Article
- Nuclear alpha NAC influences bone matrix mineralization and osteoblast maturation in vivo.Molecular and cellular biology · 2010Article
- Phosphorylation of threonine 3: implications for Huntingtin aggregation and neurotoxicity.The Journal of biological chemistry · 2009Article
- CK2 negatively regulates Galphas signaling.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- FIAT is co-expressed with its dimerization target ATF4 in early osteoblasts, but not in osteocytes.Gene expression patterns : GEP · 2009Article
- Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination.Genetics · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The subcellular localization of the alphaNAC coactivator is regulated, but the signaling pathways controlling its nucleocytoplasmic shuttling and coactivation function are not completely characterized. We report here that casein kinase II (CK2) phosphorylated alphaNAC on several phosphoacceptor sites, especially in an amino-terminal cluster. Deletion or mutation of the clustered CK2 sites induced nuclear accumulation of alphaNAC in cells. alphaNAC also localized to the nucleus when endogenous CK2 activity was inhibited by quercetin or 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB). These observations suggested that phosphorylation by CK2 might play a signaling role in the nuclear export of alphaNAC. Interestingly, inhibition of the chromosome region maintenance 1 (CRM1) exportin by leptomycin B (LMB) led to accumulation of alphaNAC in the nucleus. We conclude that CK2 phosphorylation of the N-terminal cluster corresponds to the signal for alphaNAC's nuclear export via a CRM1-dependent pathway. Finally, the nuclear accumulation of the protein resulting from the lack of CK2 phosphorylation mediated a slight but significant increase of the alphaNAC coactivating function on AP-1 transcriptional activity. Thus, alphaNAC's exit from the nucleus and capacity to potentiate transcription appear dependent on its phosphorylation status.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.