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Expanding the interactome of TES by exploiting TES modules with different subcellular localizations

Stefano Sala UGent, Marleen Van Troys UGent, Sandrine Medves, Marie Catillon, Evy Timmerman UGent, An Staes UGent, Elisabeth Schaffner-Reckinger, Kris Gevaert UGent and Christophe Ampe UGent (2017) JOURNAL OF PROTEOME RESEARCH. 16(5). p.2054-2071
abstract
The multimodular nature of many eukaryotic proteins underlies their temporal or spatial engagement in a range of protein cocomplexes. Using the multimodule protein testin (TES), we here report a proteomics approach to increase insight in cocomplex diversity. The LIM-domain containing and tumor suppressor protein TES is present at different actin cytoskeleton adhesion structures in cells and influences cell migration, adhesion and spreading. TES module accessibility has been proposed to vary due to conformational switching and variants of TES lacking specific domains target to different subcellular locations. By applying iMixPro AP-MS ("intelligent Mixing of Proteomes"-affinity purification-mass spectrometry) to a set of tagged-TES modular variants, we identified proteins residing in module-specific cocomplexes. The obtained distinct module-specific interactomes combine to a global TES interactome that becomes more extensive and richer in information. Applying pathway analysis to the module interactomes revealed expected actin-related canonical pathways and also less expected pathways. We validated two new TES cocomplex partners: TGFB1I1 and a short form of the glucocorticoid receptor. TES and TGFB1I1 are shown to oppositely affect cell spreading providing biological validity for their copresence in complexes since they act in similar processes.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
actin, affinity purification-mass spectrometry, cell spreading, focal adhesion, glucocorticoid receptor, pathway analysis, protein-protein interaction, transforming growth factor beta 1 induced 1, VASP, Zyxin, PURIFICATION-MASS SPECTROMETRY, ACTIN-BINDING PROTEINS, FOCAL ADHESION PROTEIN, LIM DOMAIN PROTEIN, GLUCOCORTICOID-RECEPTOR, DEXAMETHASONE, CYTOSKELETON, MOTILITY, CANCER, TALIN
journal title
JOURNAL OF PROTEOME RESEARCH
J. Proteome Res.
volume
16
issue
5
pages
2054 - 2071
Web of Science type
Article
Web of Science id
000401044600020
ISSN
1535-3893
1535-3907
DOI
10.1021/acs.jproteome.7b00034
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
8519249
handle
http://hdl.handle.net/1854/LU-8519249
date created
2017-05-02 13:45:08
date last changed
2017-07-05 08:04:19
@article{8519249,
  abstract     = {The multimodular nature of many eukaryotic proteins underlies their temporal or spatial engagement in a range of protein cocomplexes. Using the multimodule protein testin (TES), we here report a proteomics approach to increase insight in cocomplex diversity. The LIM-domain containing and tumor suppressor protein TES is present at different actin cytoskeleton adhesion structures in cells and influences cell migration, adhesion and spreading. TES module accessibility has been proposed to vary due to conformational switching and variants of TES lacking specific domains target to different subcellular locations. By applying iMixPro AP-MS ({\textacutedbl}intelligent Mixing of Proteomes{\textacutedbl}-affinity purification-mass spectrometry) to a set of tagged-TES modular variants, we identified proteins residing in module-specific cocomplexes. The obtained distinct module-specific interactomes combine to a global TES interactome that becomes more extensive and richer in information. Applying pathway analysis to the module interactomes revealed expected actin-related canonical pathways and also less expected pathways. We validated two new TES cocomplex partners: TGFB1I1 and a short form of the glucocorticoid receptor. TES and TGFB1I1 are shown to oppositely affect cell spreading providing biological validity for their copresence in complexes since they act in similar processes.},
  author       = {Sala, Stefano and Van Troys, Marleen and Medves, Sandrine and Catillon, Marie and Timmerman, Evy and Staes, An and Schaffner-Reckinger, Elisabeth and Gevaert, Kris and Ampe, Christophe},
  issn         = {1535-3893},
  journal      = {JOURNAL OF PROTEOME RESEARCH},
  keyword      = {actin,affinity purification-mass spectrometry,cell spreading,focal adhesion,glucocorticoid receptor,pathway analysis,protein-protein interaction,transforming growth factor beta 1 induced 1,VASP,Zyxin,PURIFICATION-MASS SPECTROMETRY,ACTIN-BINDING PROTEINS,FOCAL ADHESION PROTEIN,LIM DOMAIN PROTEIN,GLUCOCORTICOID-RECEPTOR,DEXAMETHASONE,CYTOSKELETON,MOTILITY,CANCER,TALIN},
  language     = {eng},
  number       = {5},
  pages        = {2054--2071},
  title        = {Expanding the interactome of TES by exploiting TES modules with different subcellular localizations},
  url          = {http://dx.doi.org/10.1021/acs.jproteome.7b00034},
  volume       = {16},
  year         = {2017},
}

Chicago
Sala, Stefano, Marleen Van Troys, Sandrine Medves, Marie Catillon, Evy Timmerman, An Staes, Elisabeth Schaffner-Reckinger, Kris Gevaert, and Christophe Ampe. 2017. “Expanding the Interactome of TES by Exploiting TES Modules with Different Subcellular Localizations.” Journal of Proteome Research 16 (5): 2054–2071.
APA
Sala, S., Van Troys, M., Medves, S., Catillon, M., Timmerman, E., Staes, A., Schaffner-Reckinger, E., et al. (2017). Expanding the interactome of TES by exploiting TES modules with different subcellular localizations. JOURNAL OF PROTEOME RESEARCH, 16(5), 2054–2071.
Vancouver
1.
Sala S, Van Troys M, Medves S, Catillon M, Timmerman E, Staes A, et al. Expanding the interactome of TES by exploiting TES modules with different subcellular localizations. JOURNAL OF PROTEOME RESEARCH. 2017;16(5):2054–71.
MLA
Sala, Stefano, Marleen Van Troys, Sandrine Medves, et al. “Expanding the Interactome of TES by Exploiting TES Modules with Different Subcellular Localizations.” JOURNAL OF PROTEOME RESEARCH 16.5 (2017): 2054–2071. Print.