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

Bullock, AN; Das, S; Debreczeni, JE; Rellos, P; Fedorov, O; Niesen, FH; Guo, K; Papagrigoriou, E; Amos, AL; Cho, S; Turk, BE; Ghosh, G; Knapp, S

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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APA Style

Bullock, A. N., Das, S., Debreczeni, J. E., Rellos, P., Fedorov, O., Niesen, F. H., Guo, K., Papagrigoriou, E., Amos, A. L., Cho, S., Turk, B. E., Ghosh, G., & Knapp, S. (2009). Kinase domain insertions define distinct roles of CLK kinases in SR protein phosphorylation. Structure (London, England : 1993), 17(3), 352–362.

MLA Style

Bullock, A. N., et al. “Kinase Domain Insertions Define Distinct Roles of CLK Kinases in SR Protein Phosphorylation.” Structure (London, England : 1993), vol. 17, no. 3, Structure (London, England : 1993), 2009, pp. 352–62.

Chicago Style

Bullock, AN, S Das, JE Debreczeni, P Rellos, O Fedorov, FH Niesen, K Guo, et al. 2009. “Kinase Domain Insertions Define Distinct Roles of CLK Kinases in SR Protein Phosphorylation.” Structure (London, England : 1993) 17 (3): 352–62.
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