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 ... [truncated at 450 characters in length]|
|Author||Bullock, Alex N; Das, Sanjan; Debreczeni, Judit E; et al|
|Subject||Amino Acid Sequence Binding Sites Humans Models, Molecular Molecular Sequence Data Mutagenesis, Insertional Nuclear Proteins Phosphorylation Protein Conformation Protein Structure, Tertiary Protein-Serine-Threonine Kinases Protein-Tyrosine Kinases RNA Splicing RNA-Binding Proteins Substrate Specificity chemistry metabolism chemistry metabolism chemistry metabolism chemistry metabolism|