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

(2017) JOURNAL OF PROTEOME RESEARCH. 16(5). p.2054-2071
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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.
Keywords
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

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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.
@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},
}

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