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

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

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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

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