AGC Kinases in mTOR signaling

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The mammalian target of rapamycin (mTOR), a protein kinase with homology to lipid kinases, orchestrates cellular responses to growth and stress signals. Various extracellular and intracellular inputs to mTOR are known. mTOR processes these inputs as part of two mTOR protein complexes, mTORC1 or mTORC2. Surprisingly, despite the many cellular functions that are linked to mTOR, there are very few direct mTOR substrates identified to date. With the recent discovery of mTORC2, mounting evidence point to mTOR as a central regulator of members of a family of protein kinases, the AGC (protein kinases A/PKG/PKC) family. The AGC kinases are one of the most well-characterized among the eukaryotic protein kinase family. A multitude of cellular functions and substrates has been ascribed to these kinases and their deregulation underlies numerous pathological conditions. mTOR phosphorylates common motifs in a number of these AGC kinases that could lead to their allosteric activation. AGC kinase activation triggers the phosphorylation of diverse targets that ultimately control cellular response to stimuli. This review will focus on the recent findings on how mTOR regulates AGC kinases. I will discuss how these kinases are wired to the mTOR signaling circuit, including examples of mTOR-dependent outputs consequent to AGC kinase activation.

Original languageEnglish (US)
Title of host publicationEnzymes
PublisherAcademic Press
Pages101-128
Number of pages28
EditionC
DOIs
StatePublished - Jan 1 2010

Publication series

NameEnzymes
NumberC
Volume27
ISSN (Print)1874-6047

Fingerprint

Sirolimus
Phosphotransferases
TOR Serine-Threonine Kinases
Protein Kinases
Chemical activation
Phosphorylation
Deregulation
Cyclic AMP-Dependent Protein Kinases
Substrates
Mountings
Lipids
Networks (circuits)
Growth

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Jacinto, E. (2010). AGC Kinases in mTOR signaling. In Enzymes (C ed., pp. 101-128). (Enzymes; Vol. 27, No. C). Academic Press. https://doi.org/10.1016/S1874-6047(10)27007-5
Jacinto, Estela. / AGC Kinases in mTOR signaling. Enzymes. C. ed. Academic Press, 2010. pp. 101-128 (Enzymes; C).
@inbook{f5b0bfe0884f4538a68e4c2a79be732d,
title = "AGC Kinases in mTOR signaling",
abstract = "The mammalian target of rapamycin (mTOR), a protein kinase with homology to lipid kinases, orchestrates cellular responses to growth and stress signals. Various extracellular and intracellular inputs to mTOR are known. mTOR processes these inputs as part of two mTOR protein complexes, mTORC1 or mTORC2. Surprisingly, despite the many cellular functions that are linked to mTOR, there are very few direct mTOR substrates identified to date. With the recent discovery of mTORC2, mounting evidence point to mTOR as a central regulator of members of a family of protein kinases, the AGC (protein kinases A/PKG/PKC) family. The AGC kinases are one of the most well-characterized among the eukaryotic protein kinase family. A multitude of cellular functions and substrates has been ascribed to these kinases and their deregulation underlies numerous pathological conditions. mTOR phosphorylates common motifs in a number of these AGC kinases that could lead to their allosteric activation. AGC kinase activation triggers the phosphorylation of diverse targets that ultimately control cellular response to stimuli. This review will focus on the recent findings on how mTOR regulates AGC kinases. I will discuss how these kinases are wired to the mTOR signaling circuit, including examples of mTOR-dependent outputs consequent to AGC kinase activation.",
author = "Estela Jacinto",
year = "2010",
month = "1",
day = "1",
doi = "10.1016/S1874-6047(10)27007-5",
language = "English (US)",
series = "Enzymes",
publisher = "Academic Press",
number = "C",
pages = "101--128",
booktitle = "Enzymes",
address = "United Kingdom",
edition = "C",

}

Jacinto, E 2010, AGC Kinases in mTOR signaling. in Enzymes. C edn, Enzymes, no. C, vol. 27, Academic Press, pp. 101-128. https://doi.org/10.1016/S1874-6047(10)27007-5

AGC Kinases in mTOR signaling. / Jacinto, Estela.

Enzymes. C. ed. Academic Press, 2010. p. 101-128 (Enzymes; Vol. 27, No. C).

Research output: Chapter in Book/Report/Conference proceedingChapter

TY - CHAP

T1 - AGC Kinases in mTOR signaling

AU - Jacinto, Estela

PY - 2010/1/1

Y1 - 2010/1/1

N2 - The mammalian target of rapamycin (mTOR), a protein kinase with homology to lipid kinases, orchestrates cellular responses to growth and stress signals. Various extracellular and intracellular inputs to mTOR are known. mTOR processes these inputs as part of two mTOR protein complexes, mTORC1 or mTORC2. Surprisingly, despite the many cellular functions that are linked to mTOR, there are very few direct mTOR substrates identified to date. With the recent discovery of mTORC2, mounting evidence point to mTOR as a central regulator of members of a family of protein kinases, the AGC (protein kinases A/PKG/PKC) family. The AGC kinases are one of the most well-characterized among the eukaryotic protein kinase family. A multitude of cellular functions and substrates has been ascribed to these kinases and their deregulation underlies numerous pathological conditions. mTOR phosphorylates common motifs in a number of these AGC kinases that could lead to their allosteric activation. AGC kinase activation triggers the phosphorylation of diverse targets that ultimately control cellular response to stimuli. This review will focus on the recent findings on how mTOR regulates AGC kinases. I will discuss how these kinases are wired to the mTOR signaling circuit, including examples of mTOR-dependent outputs consequent to AGC kinase activation.

AB - The mammalian target of rapamycin (mTOR), a protein kinase with homology to lipid kinases, orchestrates cellular responses to growth and stress signals. Various extracellular and intracellular inputs to mTOR are known. mTOR processes these inputs as part of two mTOR protein complexes, mTORC1 or mTORC2. Surprisingly, despite the many cellular functions that are linked to mTOR, there are very few direct mTOR substrates identified to date. With the recent discovery of mTORC2, mounting evidence point to mTOR as a central regulator of members of a family of protein kinases, the AGC (protein kinases A/PKG/PKC) family. The AGC kinases are one of the most well-characterized among the eukaryotic protein kinase family. A multitude of cellular functions and substrates has been ascribed to these kinases and their deregulation underlies numerous pathological conditions. mTOR phosphorylates common motifs in a number of these AGC kinases that could lead to their allosteric activation. AGC kinase activation triggers the phosphorylation of diverse targets that ultimately control cellular response to stimuli. This review will focus on the recent findings on how mTOR regulates AGC kinases. I will discuss how these kinases are wired to the mTOR signaling circuit, including examples of mTOR-dependent outputs consequent to AGC kinase activation.

UR - http://www.scopus.com/inward/record.url?scp=77954909105&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77954909105&partnerID=8YFLogxK

U2 - 10.1016/S1874-6047(10)27007-5

DO - 10.1016/S1874-6047(10)27007-5

M3 - Chapter

AN - SCOPUS:77954909105

T3 - Enzymes

SP - 101

EP - 128

BT - Enzymes

PB - Academic Press

ER -

Jacinto E. AGC Kinases in mTOR signaling. In Enzymes. C ed. Academic Press. 2010. p. 101-128. (Enzymes; C). https://doi.org/10.1016/S1874-6047(10)27007-5