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PMID:26683827
Citation |
Marstad, A, Landsverk, OJ, Strømme, O, Otterlei, M, Collas, P, Sundan, A and Brede, G (2016) A-kinase anchoring protein AKAP95 is a novel regulator of ribosomal RNA synthesis. FEBS J. 283:757-70 |
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Abstract |
The RNA polymerase I transcription apparatus acquires and integrates the combined information from multiple cellular signalling cascades to regulate ribosome production essential for cell growth and proliferation. In the present study, we show that a subpopulation of A-kinase anchoring protein 95 (AKAP95) targets the nucleolus during interphase and is involved in regulating rRNA production. We show that AKAP95 co-localizes with the nucleolar upstream binding factor, an essential rRNA transcription factor. Similar to other members of the C2 H2 -zinc finger family, we show, using systematic selection and evolution of ligands by exponential enrichment and in vitro binding analysis, that AKAP95 has a preference for GC-rich DNA in vitro, whereas fluorescence recovery after photobleaching analysis reveals AKAP95 to be a highly mobile protein that exhibits RNA polymerase I and II dependent nucleolar trafficking. In line with its GC-binding features, chromatin immunoprecipitation analysis revealed AKAP95 to be associated with ribosomal chromatin in vivo. Manipulation of AKAP95-expression in U2OS cells revealed a reciprocal relationship between the expression of AKAP95 and 47S rRNA. Taken together, our data indicate that AKAP95 is a novel nucleolus-associated protein with a regulatory role on rRNA production. |
Links |
PubMed Online version:10.1111/febs.13630 |
Keywords |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
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GO:0005730: nucleolus |
ECO:0000314: |
C |
Figure 1. shows the intra-nuclear localization of AKAP95 is dependent on both RNA polymerase I and RNA polymerase II. |
complete | ||||
Notes
See also
References
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