- Abstract:
-
Splicing requires reversible phosphorylation of serine/arginine-rich (SR) proteins, which direct splice site selection in eukaryotic mRNA. These phosphorylation events are dependent on SR protein (SRPK) and cdc2-like kinase (CLK) families. SRPK1 phosphorylation of splicing factors is restricted by a specific docking interaction whereas CLK activity is less constrained. To understand functional differences between splicing factor targeting kinases, we determined crystal structures of CLK1 and ...
Expand abstract - Publication status:
- Published
- Journal:
- Structure (London, England : 1993)
- Volume:
- 17
- Issue:
- 3
- Pages:
- 352-362
- Publication date:
- 2009-03-05
- DOI:
- EISSN:
-
1878-4186
- ISSN:
-
0969-2126
- URN:
-
uuid:4c42dc66-b2d9-4b44-843e-62339be10bd7
- Source identifiers:
-
34641
- Local pid:
- pubs:34641
- Language:
- English
- Keywords:
- Copyright date:
- 2009
Journal article
Kinase domain insertions define distinct roles of CLK kinases in SR protein phosphorylation.
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