The Chemical Biology of Phosphoinositide 3-Kinases

Matthias P. Wymann, Carsten Schultz

Research output: Contribution to journalReview article

28 Citations (Scopus)

Abstract

Since its discovery in the late 1980s, phosphoinositide 3-kinase (PI3K), and its isoforms have arguably reached the forefront of signal transduction research. Regulation of this lipid kinase, its functions, its effectors, in short its entire signaling network, has been extensively studied. PI3K inhibitors are frequently used in biochemistry and cell biology. In addition, many pharmaceutical companies have launched drug-discovery programs to identify modulators of PI3Ks. Despite these efforts and a fairly good knowledge of the PI3K signaling network, we still have only a rudimentary picture of the signaling dynamics of PI3K and its lipid products in space and time. It is therefore essential to create and use novel biological and chemical tools to manipulate the phosphoinositide signaling network with spatial and temporal resolution. In this review, we discuss the current and potential future tools that are available and necessary to unravel the various functions of PI3K and its isoforms.

Original languageEnglish (US)
Pages (from-to)2022-2035
Number of pages14
JournalChemBioChem
Volume13
Issue number14
DOIs
StatePublished - Sep 24 2012
Externally publishedYes

Fingerprint

1-Phosphatidylinositol 4-Kinase
Phosphatidylinositols
Phosphotransferases
Protein Isoforms
Lipids
Cytology
Drug Discovery
Signal transduction
Biochemistry
Phosphatidylinositol 3-Kinases
Cell Biology
Signal Transduction
Modulators
Research
Pharmaceutical Preparations
Industry

Keywords

  • Phosphoinositide 3-kinase
  • PI3K inhibitors
  • Rapamycin
  • Signaling pathways
  • Wortmannin

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Molecular Medicine
  • Molecular Biology

Cite this

The Chemical Biology of Phosphoinositide 3-Kinases. / Wymann, Matthias P.; Schultz, Carsten.

In: ChemBioChem, Vol. 13, No. 14, 24.09.2012, p. 2022-2035.

Research output: Contribution to journalReview article

Wymann, Matthias P. ; Schultz, Carsten. / The Chemical Biology of Phosphoinositide 3-Kinases. In: ChemBioChem. 2012 ; Vol. 13, No. 14. pp. 2022-2035.
@article{83118eeb4adf468189c7e0f321604cc1,
title = "The Chemical Biology of Phosphoinositide 3-Kinases",
abstract = "Since its discovery in the late 1980s, phosphoinositide 3-kinase (PI3K), and its isoforms have arguably reached the forefront of signal transduction research. Regulation of this lipid kinase, its functions, its effectors, in short its entire signaling network, has been extensively studied. PI3K inhibitors are frequently used in biochemistry and cell biology. In addition, many pharmaceutical companies have launched drug-discovery programs to identify modulators of PI3Ks. Despite these efforts and a fairly good knowledge of the PI3K signaling network, we still have only a rudimentary picture of the signaling dynamics of PI3K and its lipid products in space and time. It is therefore essential to create and use novel biological and chemical tools to manipulate the phosphoinositide signaling network with spatial and temporal resolution. In this review, we discuss the current and potential future tools that are available and necessary to unravel the various functions of PI3K and its isoforms.",
keywords = "Phosphoinositide 3-kinase, PI3K inhibitors, Rapamycin, Signaling pathways, Wortmannin",
author = "Wymann, {Matthias P.} and Carsten Schultz",
year = "2012",
month = "9",
day = "24",
doi = "10.1002/cbic.201200089",
language = "English (US)",
volume = "13",
pages = "2022--2035",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley-VCH Verlag",
number = "14",

}

TY - JOUR

T1 - The Chemical Biology of Phosphoinositide 3-Kinases

AU - Wymann, Matthias P.

AU - Schultz, Carsten

PY - 2012/9/24

Y1 - 2012/9/24

N2 - Since its discovery in the late 1980s, phosphoinositide 3-kinase (PI3K), and its isoforms have arguably reached the forefront of signal transduction research. Regulation of this lipid kinase, its functions, its effectors, in short its entire signaling network, has been extensively studied. PI3K inhibitors are frequently used in biochemistry and cell biology. In addition, many pharmaceutical companies have launched drug-discovery programs to identify modulators of PI3Ks. Despite these efforts and a fairly good knowledge of the PI3K signaling network, we still have only a rudimentary picture of the signaling dynamics of PI3K and its lipid products in space and time. It is therefore essential to create and use novel biological and chemical tools to manipulate the phosphoinositide signaling network with spatial and temporal resolution. In this review, we discuss the current and potential future tools that are available and necessary to unravel the various functions of PI3K and its isoforms.

AB - Since its discovery in the late 1980s, phosphoinositide 3-kinase (PI3K), and its isoforms have arguably reached the forefront of signal transduction research. Regulation of this lipid kinase, its functions, its effectors, in short its entire signaling network, has been extensively studied. PI3K inhibitors are frequently used in biochemistry and cell biology. In addition, many pharmaceutical companies have launched drug-discovery programs to identify modulators of PI3Ks. Despite these efforts and a fairly good knowledge of the PI3K signaling network, we still have only a rudimentary picture of the signaling dynamics of PI3K and its lipid products in space and time. It is therefore essential to create and use novel biological and chemical tools to manipulate the phosphoinositide signaling network with spatial and temporal resolution. In this review, we discuss the current and potential future tools that are available and necessary to unravel the various functions of PI3K and its isoforms.

KW - Phosphoinositide 3-kinase

KW - PI3K inhibitors

KW - Rapamycin

KW - Signaling pathways

KW - Wortmannin

UR - http://www.scopus.com/inward/record.url?scp=84866443275&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84866443275&partnerID=8YFLogxK

U2 - 10.1002/cbic.201200089

DO - 10.1002/cbic.201200089

M3 - Review article

C2 - 22965647

AN - SCOPUS:84866443275

VL - 13

SP - 2022

EP - 2035

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 14

ER -