Regulation of class IA PI3Ks

H. Wu; Y. Yan; J. M. Backer

doi:10.1042/BST0350242

Regulation of class IA PI3Ks

H. Wu, Y. Yan, J. M. Backer

Molecular Pharmacology

Research output: Contribution to journal › Article › peer-review

33 Scopus citations

Abstract

Class IA PI3KS (phosphoinositide 3-kinases) regulate a wide range of cellular responses through the production of PI(3,4,5)P₃ (phosphatidylinositol 3,4,5-trisphosphate) in cellular membranes. They are activated by receptor tyrosine kinases, by Ras and Rho family GTPases, and in some cases by G_βγ subunits from trimeric G-proteins. Crystallographic studies on the related class IB PI3K_γ, and biochemical and structural studies on the class IA PI3Ks, have led to new insights into how these critical enzymes are regulated in normal cells and how mutations can lead to their constitutive activation in transformed cells. The present paper will discuss recent studies on the regulation of class I (p85/p110) PI3Ks, with a focus on the role of SH2 domains (Src homology 2 domains) in the p85 regulatory subunit in modulating PI3K activity.

Original language	English (US)
Pages (from-to)	242-244
Number of pages	3
Journal	Biochemical Society transactions
Volume	35
Issue number	2
DOIs	https://doi.org/10.1042/BST0350242
State	Published - Apr 2007

Keywords

Adaptor-binding domain (ABD)
Breakpoint cluster region (BCR)
Domain structure
Phosphoinositide 3-kinase (PI3K)
Src homology 2 domain (SH2 domain)
p85

ASJC Scopus subject areas

Biochemistry

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10.1042/BST0350242

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title = "Regulation of class IA PI3Ks",

abstract = "Class IA PI3KS (phosphoinositide 3-kinases) regulate a wide range of cellular responses through the production of PI(3,4,5)P3 (phosphatidylinositol 3,4,5-trisphosphate) in cellular membranes. They are activated by receptor tyrosine kinases, by Ras and Rho family GTPases, and in some cases by Gβγ subunits from trimeric G-proteins. Crystallographic studies on the related class IB PI3Kγ, and biochemical and structural studies on the class IA PI3Ks, have led to new insights into how these critical enzymes are regulated in normal cells and how mutations can lead to their constitutive activation in transformed cells. The present paper will discuss recent studies on the regulation of class I (p85/p110) PI3Ks, with a focus on the role of SH2 domains (Src homology 2 domains) in the p85 regulatory subunit in modulating PI3K activity.",

keywords = "Adaptor-binding domain (ABD), Breakpoint cluster region (BCR), Domain structure, Phosphoinositide 3-kinase (PI3K), Src homology 2 domain (SH2 domain), p85",

author = "H. Wu and Y. Yan and Backer, {J. M.}",

year = "2007",

month = apr,

doi = "10.1042/BST0350242",

language = "English (US)",

volume = "35",

pages = "242--244",

journal = "Biochemical Society transactions",

issn = "0300-5127",

publisher = "Portland Press Ltd.",

number = "2",

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AU - Wu, H.

AU - Yan, Y.

AU - Backer, J. M.

PY - 2007/4

Y1 - 2007/4

N2 - Class IA PI3KS (phosphoinositide 3-kinases) regulate a wide range of cellular responses through the production of PI(3,4,5)P3 (phosphatidylinositol 3,4,5-trisphosphate) in cellular membranes. They are activated by receptor tyrosine kinases, by Ras and Rho family GTPases, and in some cases by Gβγ subunits from trimeric G-proteins. Crystallographic studies on the related class IB PI3Kγ, and biochemical and structural studies on the class IA PI3Ks, have led to new insights into how these critical enzymes are regulated in normal cells and how mutations can lead to their constitutive activation in transformed cells. The present paper will discuss recent studies on the regulation of class I (p85/p110) PI3Ks, with a focus on the role of SH2 domains (Src homology 2 domains) in the p85 regulatory subunit in modulating PI3K activity.

AB - Class IA PI3KS (phosphoinositide 3-kinases) regulate a wide range of cellular responses through the production of PI(3,4,5)P3 (phosphatidylinositol 3,4,5-trisphosphate) in cellular membranes. They are activated by receptor tyrosine kinases, by Ras and Rho family GTPases, and in some cases by Gβγ subunits from trimeric G-proteins. Crystallographic studies on the related class IB PI3Kγ, and biochemical and structural studies on the class IA PI3Ks, have led to new insights into how these critical enzymes are regulated in normal cells and how mutations can lead to their constitutive activation in transformed cells. The present paper will discuss recent studies on the regulation of class I (p85/p110) PI3Ks, with a focus on the role of SH2 domains (Src homology 2 domains) in the p85 regulatory subunit in modulating PI3K activity.

KW - Adaptor-binding domain (ABD)

KW - Breakpoint cluster region (BCR)

KW - Domain structure

KW - Phosphoinositide 3-kinase (PI3K)

KW - Src homology 2 domain (SH2 domain)

KW - p85

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U2 - 10.1042/BST0350242

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SP - 242

EP - 244

JO - Biochemical Society transactions

JF - Biochemical Society transactions

IS - 2

ER -

Regulation of class IA PI3Ks

Abstract

Keywords

ASJC Scopus subject areas

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