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  Phospho-tyrosine dependent protein-protein interaction network

Grossmann, A., Benlasfer, N., Birth, P., Hegele, A. K., Wachsmuth, F., Apelt, L., et al. (2015). Phospho-tyrosine dependent protein-protein interaction network. Molecular Systems Biology, 11(3): 0794. doi:10.15252/msb.20145968.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-5FDA-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-5FDB-1
Genre: Journal Article

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 Creators:
Grossmann, Arndt1, Author              
Benlasfer, Nouhad1, Author              
Birth, Petra2, Author              
Hegele, Anna K.2, Author              
Wachsmuth, Franziska2, Author
Apelt, Luise1, Author              
Stelzl, Ulrich1, Author              
Affiliations:
1Molecular Interaction Networks (Ulrich Stelzl), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479660              
2Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433554              

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Free keywords: cancer signaling network biology post-translational protein modification yeast two-hybrid
 Abstract: Post-translational protein modifications, such as tyrosine phosphorylation, regulate protein-protein interactions (PPIs) critical for signal processing and cellular phenotypes. We extended an established yeast two-hybrid system employing human protein kinases for the analyses of phospho-tyrosine (pY)-dependent PPIs in a direct experimental, large-scale approach. We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins and validated a large fraction in co-immunoprecipitation experiments from mammalian cells. About one-sixth of the interactions are mediated by known linear sequence binding motifs while the majority of pY-PPIs are mediated by other linear epitopes or governed by alternative recognition modes. Network analysis revealed that pY-mediated recognition events are tied to a highly connected protein module dedicated to signaling and cell growth pathways related to cancer. Using binding assays, protein complementation and phenotypic readouts to characterize the pY-dependent interactions of TSPAN2 (tetraspanin 2) and GRB2 or PIK3R3 (p55gamma), we exemplarily provide evidence that the two pY-dependent PPIs dictate cellular cancer phenotypes.

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Language(s): eng - English
 Dates: 2015-03-26
 Publication Status: Published online
 Pages: -
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 Identifiers: DOI: 10.15252/msb.20145968
ISSN: 1744-4292 (Electronic)
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Title: Molecular Systems Biology
Source Genre: Journal
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Publ. Info: London : Nature Pub. Group
Pages: - Volume / Issue: 11 (3) Sequence Number: 0794 Start / End Page: - Identifier: ISSN: 1744-4292
CoNE: /journals/resource/1000000000021290