Similarity between phospholipase C and the regulatory domain of protein kinase C.

Abstract

We report that a 100 residue segment in the carboxy-terminus half of phosphatidylinositol-specific phospholipase C is similar to a segment in the amino-terminus half of protein kinase C. The computer-based comparison score is 9.5 standard deviations higher than that of 2500 comparisons of randomized sequences of these segments (P = 10(-21), suggesting that the two segments have similar biological properties. Phospholipase C has a segment that is homologous to part of the non-catalytic domain of src kinase and other tyrosine protein kinases. The similarity of phospholipase C with protein kinase C, a serine/threonine kinase suggests that novel exon shuffling occurred among serine/threonine and tyrosine kinases and phospholipase C.

Cite this paper

@article{Baker1989SimilarityBP, title={Similarity between phospholipase C and the regulatory domain of protein kinase C.}, author={Michael E. Baker}, journal={Molecular and cellular endocrinology}, year={1989}, volume={61 1}, pages={129-31} }