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 (Clifton, N.J.) |
| Volume | 1298 |
| DOIs | |
| State | Published - 2015 |
| Externally published | Yes |
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Keywords
- Class IA PI 3-kinase
- Lipid kinases
- P110beta
- Phosphoinositide 3-kinases
- PIK3CB
- Rab5
- Small GTPases
ASJC Scopus subject areas
- Molecular Biology
- Genetics
Cite this
Identification of the rab5 binding site in p110β : Assays for pi3kβ binding to rab5. / Salamon, Rachel S.; Dbouk, Hashem A.; Collado, Denise; Lopiccolo, Jaclyn; Bresnick, Anne R.; Backer, Jonathan M.
In: Methods in molecular biology (Clifton, N.J.), Vol. 1298, 2015, p. 271-281.Research output: Contribution to journal › Article
}
TY - JOUR
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, Jonathan 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 - Phosphoinositide 3-kinases
KW - PIK3CB
KW - Rab5
KW - Small GTPases
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UR - http://www.scopus.com/inward/citedby.url?scp=84925954830&partnerID=8YFLogxK
U2 - 10.1007/978-1-4939-2569-8_23
DO - 10.1007/978-1-4939-2569-8_23
M3 - Article
VL - 1298
SP - 271
EP - 281
JO - Methods in Molecular Biology
JF - Methods in Molecular Biology
SN - 1064-3745
ER -