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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

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Publisher copy:
10.1016/j.str.2008.12.023

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Debreczeni, JE More by this author
Fedorov, O More by this author
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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

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