Back to Search
Start Over
Inhibition of Spliceosome Assembly by the Cell Cycle-regulated Protein Kinase MELK and Involvement of Splicing Factor NIPP1.
- Source :
-
Journal of Biological Chemistry . 3/5/2004, Vol. 279 Issue 10, p8642-8647. 6p. 4 Diagrams, 2 Graphs. - Publication Year :
- 2004
-
Abstract
- NIPP1 is a ubiquitous nuclear protein that is required for spliceosome assembly. We report here that the phosphothreonine-binding Forkhead-associated domain of NIPP1 interacts with the cell cycle-regulated protein Ser/Thr kinase MELK (maternal embryonic leucine zipper kinase). The NIPP1-MELK interaction was critically dependent on the phosphorylaton of Thr-478 of MELK and was increased in lysates from mitotically arrested cells. Recombinant MELK was a potent inhibitor of an early step of spliceosome assembly in nuclear extracts. This splicing defect was also seen with a kinase-dead mutant but was absent after mutation (T478A) of the NIPP1 binding site of MELK, indicating a mediatory role for NIPP1. Our data suggest that MELK has a role in the cell cycle-regulated control of pre-mRNA splicing. [ABSTRACT FROM AUTHOR]
- Subjects :
- *PROTEINS
*CELL cycle
*LEUCINE
*MESSENGER RNA
*CELLS
Subjects
Details
- Language :
- English
- ISSN :
- 00219258
- Volume :
- 279
- Issue :
- 10
- Database :
- Academic Search Index
- Journal :
- Journal of Biological Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 12732317
- Full Text :
- https://doi.org/10.1074/jbc.M311466200