Serine/threonine phosphorylation regulates binding of C hnRNP proteins to pre-mRNA.
basic_science · Level V
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- Record sourced from PubMed, PMID 8356082.
- Also identified by PMC identifier 47223.
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Abstract
The C hnRNP proteins bind to nascent pre-mRNA and are thought to participate in an early step of the pre-mRNA splicing pathway. We report here that C hnRNP proteins are phosphorylated by a casein kinase II activity in a HeLa cell nuclear extract and that dephosphorylation of C hnRNP proteins is inhibited by the specific protein-serine/threonine-phosphatase 1/2A inhibitor okadaic acid. We further find that dephosphorylation of C hnRNP proteins is required for their binding to adenovirus and human beta-globin pre-mRNAs. These results indicate that the participation of C hnRNP proteins in pre-spliceosome assembly is coupled to a dynamic cycle of their phosphorylation and dephosphorylation.
Medical subject headings
- Protein Serine-Threonine Kinases
- RNA Precursors
- RNA, Heterogeneous Nuclear
- Ribonucleoproteins