Key result
Protein Kinase Cδ phosphorylates the heterogeneous nuclear ribonucleoprotein K protein at Ser302, and their interaction is greatly increased by K protein phosphorylation on tyrosine residues.
Population
In vitro models and COS cells
Design
Preclinical
Authors
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No immediate clinical implications; leaves open PKCδ-hnRNP K roles in cardiovascular signaling.
PKCδ binds and phosphorylates hnRNP K protein, an interaction regulated by tyrosine phosphorylation, which may facilitate molecular cross-talk in cellular signaling.
Schullery et al. (1999) studied this question. Protein Kinase Cδ was evaluated on Phosphorylation and interaction of K protein with PKCdelta. Protein Kinase Cδ phosphorylates the heterogeneous nuclear ribonucleoprotein K protein at Ser302, and their interaction is greatly increased by K protein phosphorylation on tyrosine residues.
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