Identification of the rab5 binding site in p110β: Assays for pi3kβ binding to rab5

Rachel S. Salamon; Hashem A. Dbouk; Denise Collado; Jaclyn Lopiccolo; Anne R. Bresnick; Jonthan M. Backer

doi:10.1007/978-1-4939-2569-8_23

Identification of the rab5 binding site in p110β: Assays for pi3kβ binding to rab5

Rachel S. Salamon, Hashem A. Dbouk, Denise Collado, Jaclyn Lopiccolo, Anne R. Bresnick, Jonthan M. Backer

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

8 Scopus citations

Abstract

Isoform-specific signaling by Class IA PI 3-kinases depends in part on the interactions between distinct catalytic subunits and upstream regulatory proteins. From among the class IA catalytic subunits (p110α, p110β, and p110δ), p110β has unique properties. Unlike the other family members, p110β directly binds to Gβγ subunits, downstream from activated G-protein coupled receptors, and to activated Rab5. Furthermore, the Ras-binding domain (RBD) of p110β binds to Rac and Cdc42 but not to Ras. Defining mutations that specifically disrupt these regulatory interactions is critical for defining their role in p110β signaling. This chapter describes the approach that was used to identify the Rab5 binding site in p110β, and discusses methods for the analysis of p110β-Rab5 interactions.

Original language	English (US)
Pages (from-to)	271-281
Number of pages	11
Journal	Methods in Molecular Biology
Volume	1298
DOIs	https://doi.org/10.1007/978-1-4939-2569-8_23
State	Published - 2015

Keywords

Class IA PI 3-kinase
Lipid kinases
P110beta
PIK3CB
Phosphoinositide 3-kinases
Rab5
Small GTPases

ASJC Scopus subject areas

Molecular Biology
Genetics

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title = "Identification of the rab5 binding site in p110β: Assays for pi3kβ binding to rab5",

abstract = "Isoform-specific signaling by Class IA PI 3-kinases depends in part on the interactions between distinct catalytic subunits and upstream regulatory proteins. From among the class IA catalytic subunits (p110α, p110β, and p110δ), p110β has unique properties. Unlike the other family members, p110β directly binds to Gβγ subunits, downstream from activated G-protein coupled receptors, and to activated Rab5. Furthermore, the Ras-binding domain (RBD) of p110β binds to Rac and Cdc42 but not to Ras. Defining mutations that specifically disrupt these regulatory interactions is critical for defining their role in p110β signaling. This chapter describes the approach that was used to identify the Rab5 binding site in p110β, and discusses methods for the analysis of p110β-Rab5 interactions.",

keywords = "Class IA PI 3-kinase, Lipid kinases, P110beta, PIK3CB, Phosphoinositide 3-kinases, Rab5, Small GTPases",

author = "Salamon, {Rachel S.} and Dbouk, {Hashem A.} and Denise Collado and Jaclyn Lopiccolo and Bresnick, {Anne R.} and Backer, {Jonthan M.}",

year = "2015",

doi = "10.1007/978-1-4939-2569-8_23",

language = "English (US)",

volume = "1298",

pages = "271--281",

journal = "Methods in Molecular Biology",

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T1 - Identification of the rab5 binding site in p110β

T2 - Assays for pi3kβ binding to rab5

AU - Salamon, Rachel S.

AU - Dbouk, Hashem A.

AU - Collado, Denise

AU - Lopiccolo, Jaclyn

AU - Bresnick, Anne R.

AU - Backer, Jonthan M.

PY - 2015

Y1 - 2015

N2 - Isoform-specific signaling by Class IA PI 3-kinases depends in part on the interactions between distinct catalytic subunits and upstream regulatory proteins. From among the class IA catalytic subunits (p110α, p110β, and p110δ), p110β has unique properties. Unlike the other family members, p110β directly binds to Gβγ subunits, downstream from activated G-protein coupled receptors, and to activated Rab5. Furthermore, the Ras-binding domain (RBD) of p110β binds to Rac and Cdc42 but not to Ras. Defining mutations that specifically disrupt these regulatory interactions is critical for defining their role in p110β signaling. This chapter describes the approach that was used to identify the Rab5 binding site in p110β, and discusses methods for the analysis of p110β-Rab5 interactions.

AB - Isoform-specific signaling by Class IA PI 3-kinases depends in part on the interactions between distinct catalytic subunits and upstream regulatory proteins. From among the class IA catalytic subunits (p110α, p110β, and p110δ), p110β has unique properties. Unlike the other family members, p110β directly binds to Gβγ subunits, downstream from activated G-protein coupled receptors, and to activated Rab5. Furthermore, the Ras-binding domain (RBD) of p110β binds to Rac and Cdc42 but not to Ras. Defining mutations that specifically disrupt these regulatory interactions is critical for defining their role in p110β signaling. This chapter describes the approach that was used to identify the Rab5 binding site in p110β, and discusses methods for the analysis of p110β-Rab5 interactions.

KW - Class IA PI 3-kinase

KW - Lipid kinases

KW - P110beta

KW - PIK3CB

KW - Phosphoinositide 3-kinases

KW - Rab5

KW - Small GTPases

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JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

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ER -

Identification of the rab5 binding site in p110β: Assays for pi3kβ binding to rab5

Abstract

Keywords

ASJC Scopus subject areas

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