Phospho-tyrosine dependent protein-protein interaction network

被引：55

作者：

Grossmann, Arndt ^{[1
]}

Benlasfer, Nouhad ^{[1
]}

Birth, Petra ^{[1
]}

Hegele, Anna ^{[1
]}

Wachsmuth, Franziska ^{[1
]}

Apelt, Luise ^{[1
]}

Stelzl, Ulrich ^{[1
]}

机构：

[1] Max Planck Inst Mol Genet, Otto Warburg Lab, D-14195 Berlin, Germany

来源：

MOLECULAR SYSTEMS BIOLOGY | 2015年 / 11卷 / 03期

关键词：

cancer signaling; network biology; post-translational protein modification; yeast two-hybrid; POSTTRANSLATIONAL MODIFICATIONS; PHOSPHATIDYLINOSITOL; 3-KINASE; SIGNALING NETWORKS; TETRASPANIN CD151; CD9; SPECIFICITY; MORPHOLOGY; DISCOVERY; MIGRATION; RESOURCE;

D O I：

10.15252/msb.20145968

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 (p55), we exemplarily provide evidence that the two pY-dependent PPIs dictate cellular cancer phenotypes.

引用

页数：14

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