The splicing factor U1-70K interacts with the SMN complex and is required for nuclear gem integrity
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25052091
DOI
10.1242/jcs.155838
PII: jcs.155838
Knihovny.cz E-resources
- Keywords
- Cajal bodies, Gems, Nuclear structure, SMN, U1 snRNP, U1-70K,
- MeSH
- Gemini of Coiled Bodies chemistry metabolism MeSH
- Cell Nucleus chemistry genetics metabolism MeSH
- HeLa Cells MeSH
- Humans MeSH
- Ribonucleoprotein, U1 Small Nuclear chemistry genetics metabolism MeSH
- SMN Complex Proteins genetics metabolism MeSH
- RNA Splicing MeSH
- Protein Transport MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Ribonucleoprotein, U1 Small Nuclear MeSH
- SMN Complex Proteins MeSH
- SNRNP70 protein, human MeSH Browser
The nuclear SMN complex localizes to specific structures called nuclear gems. The loss of gems is a cellular marker for several neurodegenerative diseases. Here, we identify that the U1-snRNP-specific protein U1-70K localizes to nuclear gems, and we show that U1-70K is necessary for gem integrity. Furthermore, we show that the interaction between U1-70K and the SMN complex is RNA independent, and we map the SMN complex binding site to the unstructured N-terminal tail of U1-70K. Consistent with these results, the expression of the U1-70K N-terminal tail rescues gem formation. These findings show that U1-70K is an SMN-complex-associating protein, and they suggest a new function for U1-70K in the formation of nuclear gems.
References provided by Crossref.org
Cajal bodies and snRNPs - friends with benefits
Mutations in spliceosomal proteins and retina degeneration
