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Cloning of human PRP4 reveals interaction with Clk1
1Department of Functional Genomics, Medical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan.
The Journal of Biological Chemistry
|June 22, 2001
Summary
Human PRP4 (hPRP4) is a protein kinase involved in pre-mRNA splicing. It interacts with splicing factor SF2/ASF and is regulated by Clk1 kinase, suggesting a role in signal transduction.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Prp4 is a protein kinase from Schizosaccharomyces pombe crucial for pre-mRNA splicing.
- It belongs to a kinase family that phosphorylates serine/arginine-rich proteins, including splicing factors.
Purpose of the Study:
- To clone and characterize human Prp4 (hPRP4).
- To investigate the interactions and regulatory mechanisms of hPRP4 in human cells.
Main Methods:
- Cloning of full-length hPRP4 cDNA.
- Western blot and Northern blot analyses.
- Immunofluorescence microscopy.
- In vitro kinase assays.
- Co-immunoprecipitation.
Main Results:
- hPRP4 is a 170-kDa protein ubiquitously expressed in human tissues.
- hPRP4 contains an arginine/serine-rich domain and nuclear localization signals.
- hPRP4 phosphorylates and interacts with splicing factor SF2/ASF.
- hPRP4 colocalizes with SF2/ASF in the nucleus.
- hPRP4 interacts with Clk1, and its N-terminal domain is phosphorylated by Clk1.
- Clk1 activity influences hPRP4 localization within the nucleus.
Conclusions:
- hPRP4 is a nuclear protein kinase involved in pre-mRNA splicing.
- Its interaction with SF2/ASF and regulation by Clk1 suggest a role in splicing regulation.
- The N-terminal region of hPRP4 may be regulated by Clk1 within a signal transduction pathway.