Rapid, optimized interactomic screening

Zhanna Hakhverdyan; Michal Domanski; Loren E Hough; Asha A Oroskar; Anil R Oroskar; Sarah Keegan; David J Dilworth; Kelly R Molloy; Vadim Sherman; John D Aitchison; David Fenyö; Brian T Chait; Torben Heick Jensen; Michael P Rout; John LaCava

doi:10.1038/nmeth.3395

Rapid, optimized interactomic screening

Zhanna Hakhverdyan, Michal Domanski, Loren E Hough, Asha A Oroskar, Anil R Oroskar, Sarah Keegan, David J Dilworth, Kelly R Molloy, Vadim Sherman, John D Aitchison, David Fenyö, Brian T Chait, Torben Heick Jensen, Michael P Rout, John LaCava

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Abstract

We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes.

Originalsprog	Engelsk
Tidsskrift	Nature Methods
Vol/bind	12
Nummer	6
Sider (fra-til)	553-560
Antal sider	8
ISSN	1548-7091
DOI	https://doi.org/10.1038/nmeth.3395
Status	Udgivet - jun. 2015

Adgang til dokumentet

10.1038/nmeth.3395

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4449307/

Citationsformater

@article{d56e29863854487a9c6de42800725cad,

title = "Rapid, optimized interactomic screening",

abstract = "We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes.",

author = "Zhanna Hakhverdyan and Michal Domanski and Hough, {Loren E} and Oroskar, {Asha A} and Oroskar, {Anil R} and Sarah Keegan and Dilworth, {David J} and Molloy, {Kelly R} and Vadim Sherman and Aitchison, {John D} and David Feny{\"o} and Chait, {Brian T} and Jensen, {Torben Heick} and Rout, {Michael P} and John LaCava",

year = "2015",

month = jun,

doi = "10.1038/nmeth.3395",

language = "English",

volume = "12",

pages = "553--560",

journal = "Nature Methods",

issn = "1548-7091",

publisher = "Nature Publishing Group",

number = "6",

}

TY - JOUR

T1 - Rapid, optimized interactomic screening

AU - Hakhverdyan, Zhanna

AU - Domanski, Michal

AU - Hough, Loren E

AU - Oroskar, Asha A

AU - Oroskar, Anil R

AU - Keegan, Sarah

AU - Dilworth, David J

AU - Molloy, Kelly R

AU - Sherman, Vadim

AU - Aitchison, John D

AU - Fenyö, David

AU - Chait, Brian T

AU - Jensen, Torben Heick

AU - Rout, Michael P

AU - LaCava, John

PY - 2015/6

Y1 - 2015/6

N2 - We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes.

AB - We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes.

U2 - 10.1038/nmeth.3395

DO - 10.1038/nmeth.3395

M3 - Journal article

C2 - 25938370

SN - 1548-7091

VL - 12

SP - 553

EP - 560

JO - Nature Methods

JF - Nature Methods

IS - 6

ER -

Rapid, optimized interactomic screening

Abstract

Adgang til dokumentet

Fingeraftryk

Citationsformater