@article{93c198600cac11de8478000ea68e967b,
title = "High affinity calmodulin target sequence in the signalling molecule PI 3-kinase",
abstract = "In this study we report that phosphatidylinositol 3-kinase (PI 3-kinase), a lipid kinase which participates in downstream signalling events of heterotrimeric G protein-coupled receptors and receptor tyrosine kinases, contains a high affinity binding site for calmodulin (CaM). The putative CaM-binding peptide derived from the p110gamma isoform interacts with CaM in a calcium-dependent way. Using gel shift analysis and fluorescence spectrophotometry we discovered that the peptide forms a high affinity complex with CaM. Titration experiments using dansylated CaM gave an affinity constant of 5 nM. Furthermore, a sequence comparison among different PI 3-kinase isoforms revealed that the sequence which can bind CaM is highly conserved within different PI 3-kinase isoforms. These results indicate a novel mechanism for regulating PI 3-kinase and provide a new direct link between Ca2+ and phospholipid signalling pathways.",
author = "R Fischer and J Julsgart and Berchtold, {M W}",
note = "Keywords: 1-Phosphatidylinositol 3-Kinase; Amino Acid Sequence; Calcium; Calmodulin; Molecular Sequence Data; Sequence Homology, Amino Acid; Signal Transduction; Substrate Specificity",
year = "1998",
language = "English",
volume = "425",
pages = "175--7",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1",
}