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

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...

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Bibliographic Details
Main Authors:	Bullock, A, Das, S, Debreczeni, J, Rellos, P, Fedorov, O, Niesen, F, Guo, K, Papagrigoriou, E, Amos, A, Cho, S, Turk, B, Ghosh, G, Knapp, S
Format:	Journal article
Language:	English
Published:	Cell Press 2009
Subjects:	Phosphorylation RNA-Binding Proteins Protein-Tyrosine Kinases RNA Splicing Humans Protein-Serine-Threonine Kinases Protein Structure, Tertiary metabolism Mutagenesis, Insertional Protein Conformation Nuclear Proteins Molecular Sequence Data Binding Sites Models, Molecular Amino Acid Sequence chemistry Substrate Specificity

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

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