High affinity calmodulin target sequence in the signalling molecule PI 3-kinase

FEBS Letters
R FischerM W Berchtold

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.

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Citations

May 22, 2002·Cellular Signalling·Neus AgellPriam Villalonga
Nov 6, 2013·Biochimica Et Biophysica Acta·Martin W Berchtold, Antonio Villalobo
Jun 19, 2008·Genomics, Proteomics & Bioinformatics·Yongqing Liu, Eugenia Wang
Aug 8, 2001·The Journal of Cell Biology·J EgeaJ X Comella
Jul 13, 2004·The Journal of Biological Chemistry·Tushar B DebRobert B Dickson
Mar 29, 2014·Journal of the American Society of Nephrology : JASN·Paolo FiorinaMohamed H Sayegh
Jun 25, 2003·The Journal of Biological Chemistry·Jennifer S McCullarTheresa M Filtz
May 28, 2020·International Journal of Molecular Sciences·Francesc TebarThomas Grewal
Oct 28, 2004·Biochemical Society Transactions·F J S Lee, F Liu
Jan 30, 2020·International Journal of Molecular Sciences·Antonio Villalobo, Martin W Berchtold
Dec 24, 2018·The Biochemical Journal·Antonio Villalobo
Feb 13, 2003·Biochimica Et Biophysica Acta·Claudia GentiliAna Russo de Boland
Mar 22, 2008·Cellular Signalling·Jemina MoretóFrancesc Tebar

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