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

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Standard

High affinity calmodulin target sequence in the signalling molecule PI 3-kinase. / Fischer, R; Julsgart, J; Berchtold, M W.

I: FEBS Letters, Bind 425, Nr. 1, 1998, s. 175-7.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Fischer, R, Julsgart, J & Berchtold, MW 1998, 'High affinity calmodulin target sequence in the signalling molecule PI 3-kinase', FEBS Letters, bind 425, nr. 1, s. 175-7.

APA

Fischer, R., Julsgart, J., & Berchtold, M. W. (1998). High affinity calmodulin target sequence in the signalling molecule PI 3-kinase. FEBS Letters, 425(1), 175-7.

Vancouver

Fischer R, Julsgart J, Berchtold MW. High affinity calmodulin target sequence in the signalling molecule PI 3-kinase. FEBS Letters. 1998;425(1):175-7.

Author

Fischer, R ; Julsgart, J ; Berchtold, M W. / High affinity calmodulin target sequence in the signalling molecule PI 3-kinase. I: FEBS Letters. 1998 ; Bind 425, Nr. 1. s. 175-7.

Bibtex

@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 = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - High affinity calmodulin target sequence in the signalling molecule PI 3-kinase

AU - Fischer, R

AU - Julsgart, J

AU - Berchtold, M W

N1 - Keywords: 1-Phosphatidylinositol 3-Kinase; Amino Acid Sequence; Calcium; Calmodulin; Molecular Sequence Data; Sequence Homology, Amino Acid; Signal Transduction; Substrate Specificity

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 9541031

VL - 425

SP - 175

EP - 177

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1

ER -

ID: 11175134