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Kinase Substrate Sensor (KISS), a mammalian in situ protein interaction sensor

Sam Lievens UGent, Sarah Gerlo UGent, Irma Lemmens UGent, Dries De Clercq, Martijn Risseeuw UGent, Nele Vanderroost UGent, Anne-Sophie De Smet UGent, Elien Ruyssinck UGent, Eric Chevet, Serge Van Calenbergh UGent, et al. (2014) MOLECULAR & CELLULAR PROTEOMICS. 126(16). p.3332-3342
abstract
Probably every cellular process is governed by protein-protein interaction (PPIs), which are often highly dynamic in nature being modulated by in-or external stimuli. Here we present KISS, for KInase Substrate Sensor, a mammalian two-hybrid approach designed to map intracellular PPIs and some of the dynamic features they exhibit. Benchmarking experiments indicate that in terms of sensitivity and specificity KISS is on par with other binary protein interaction technologies while being complementary with regard to the subset of PPIs it is able to detect. We used KISS to evaluate interactions between different types of proteins, including transmembrane proteins, expressed at their native subcellular location. In situ analysis of endoplasmic reticulum stress-induced clustering of the endoplasmic reticulum stress sensor ERN1 and ligand-dependent beta-arrestin recruitment to GPCRs illustrated the method's potential to study functional PPI modulation in complex cellular processes. Exploring its use as a tool for in cell evaluation of pharmacological interference with PPIs, we showed that reported effects of known GPCR antagonists and PPI inhibitors are properly recapitulated. In a three-hybrid setup, KISS was able to map interactions between small molecules and proteins. Taken together, we established KISS as a sensitive approach for in situ analysis of protein interactions and their modulation in a changing cellular context or in response to pharmacological challenges.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
YEAST 2-HYBRID SYSTEM, DRUG DISCOVERY, REVERSE-TRANSCRIPTASE, INTERACTION TRAP, HUMAN-CELLS, DYNAMICS, STRATEGIES, RECEPTOR, BINDING, REVEALS
journal title
MOLECULAR & CELLULAR PROTEOMICS
Mol. Cell. Proteomics
volume
126
issue
16
pages
3332 - 3342
Web of Science type
Article
Web of Science id
000345626400009
JCR category
BIOCHEMICAL RESEARCH METHODS
JCR impact factor
6.564 (2014)
JCR rank
5/79 (2014)
JCR quartile
1 (2014)
ISSN
1535-9476
DOI
10.1074/mcp.M114.041087
project
Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
5801031
handle
http://hdl.handle.net/1854/LU-5801031
date created
2015-01-09 11:21:20
date last changed
2016-12-19 15:40:01
@article{5801031,
  abstract     = {Probably every cellular process is governed by protein-protein interaction (PPIs), which are often highly dynamic in nature being modulated by in-or external stimuli. Here we present KISS, for KInase Substrate Sensor, a mammalian two-hybrid approach designed to map intracellular PPIs and some of the dynamic features they exhibit. Benchmarking experiments indicate that in terms of sensitivity and specificity KISS is on par with other binary protein interaction technologies while being complementary with regard to the subset of PPIs it is able to detect. We used KISS to evaluate interactions between different types of proteins, including transmembrane proteins, expressed at their native subcellular location. In situ analysis of endoplasmic reticulum stress-induced clustering of the endoplasmic reticulum stress sensor ERN1 and ligand-dependent beta-arrestin recruitment to GPCRs illustrated the method's potential to study functional PPI modulation in complex cellular processes. Exploring its use as a tool for in cell evaluation of pharmacological interference with PPIs, we showed that reported effects of known GPCR antagonists and PPI inhibitors are properly recapitulated. In a three-hybrid setup, KISS was able to map interactions between small molecules and proteins. Taken together, we established KISS as a sensitive approach for in situ analysis of protein interactions and their modulation in a changing cellular context or in response to pharmacological challenges.},
  author       = {Lievens, Sam and Gerlo, Sarah and Lemmens, Irma and De Clercq, Dries and Risseeuw, Martijn and Vanderroost, Nele and De Smet, Anne-Sophie and Ruyssinck, Elien and Chevet, Eric and Van Calenbergh, Serge and Tavernier, Jan},
  issn         = {1535-9476},
  journal      = {MOLECULAR \& CELLULAR PROTEOMICS},
  keyword      = {YEAST 2-HYBRID SYSTEM,DRUG DISCOVERY,REVERSE-TRANSCRIPTASE,INTERACTION TRAP,HUMAN-CELLS,DYNAMICS,STRATEGIES,RECEPTOR,BINDING,REVEALS},
  language     = {eng},
  number       = {16},
  pages        = {3332--3342},
  title        = {Kinase Substrate Sensor (KISS), a mammalian in situ protein interaction sensor},
  url          = {http://dx.doi.org/10.1074/mcp.M114.041087},
  volume       = {126},
  year         = {2014},
}

Chicago
Lievens, Sam, Sarah Gerlo, Irma Lemmens, Dries De Clercq, Martijn Risseeuw, Nele Vanderroost, Anne-Sophie De Smet, et al. 2014. “Kinase Substrate Sensor (KISS), a Mammalian in Situ Protein Interaction Sensor.” Molecular & Cellular Proteomics 126 (16): 3332–3342.
APA
Lievens, Sam, Gerlo, S., Lemmens, I., De Clercq, D., Risseeuw, M., Vanderroost, N., De Smet, A.-S., et al. (2014). Kinase Substrate Sensor (KISS), a mammalian in situ protein interaction sensor. MOLECULAR & CELLULAR PROTEOMICS, 126(16), 3332–3342.
Vancouver
1.
Lievens S, Gerlo S, Lemmens I, De Clercq D, Risseeuw M, Vanderroost N, et al. Kinase Substrate Sensor (KISS), a mammalian in situ protein interaction sensor. MOLECULAR & CELLULAR PROTEOMICS. 2014;126(16):3332–42.
MLA
Lievens, Sam, Sarah Gerlo, Irma Lemmens, et al. “Kinase Substrate Sensor (KISS), a Mammalian in Situ Protein Interaction Sensor.” MOLECULAR & CELLULAR PROTEOMICS 126.16 (2014): 3332–3342. Print.