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Kinase domain insertions define distinct roles of CLK kinases in SR protein phosphorylation

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 ...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.str.2008.12.023

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Publisher:
Cell Press Publisher's website
Journal:
Structure Journal website
Volume:
17
Issue:
3
Pages:
352-362
Publication date:
2009-01-01
DOI:
ISSN:
0969-2126
URN:
uuid:128af0bf-7e01-4188-b305-6295064a2571
Local pid:
SGC:19278650

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