Molecular Systems Biology
EMBO and Macmillan Publishers Limited
Biology | Life Sciences
Src homology 3 (SH3) domains bind peptides to mediate protein–protein interactions that assemble and regulate dynamic biological processes. We surveyed the repertoire of SH3 binding specificity using peptide phage display in a metazoan, the worm Caenorhabditis elegans, and discovered that it structurally mirrors that of the budding yeast Saccharomyces cerevisiae.We then mapped the worm SH3 interactome using stringent yeast two-hybrid and compared it with the equivalent map for yeast.We found that the wormSH3 interactome resembles the analogous yeast network because it is significantly enriched for proteins with roles in endocytosis. Nevertheless, orthologous SH3 domain mediated interactions are highly rewired. Our results suggest a model of network evolution where general function of the SH3 domain network is conserved over its specific form.
Network Evolution, Phage Display, Protein Interaction Conservation, SH3 Domains, Yeast Two-Hybrid
Copyright 2013 EMBO and Macmillan Publishers Limited
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Xin, Xiaofeng; Gfeller, David; Cheng, Jackie; Tonikian, Raffi; Sun, Lin; Guo, Ailan; Lopez, Lianet; Pavlenco, Alevtina; Akintobi, Adenrele; Zhang, Yingnan; Rual, Jean-Francois; Currell, Bridget; Seshagiri, Somasekar; Hao, Tong; Yang, Xinping; Shen, Yun A.; Salehi-Ashtiani, Kourosh; Li, JIngjing; Cheng, Aaron T.; Bouamalay, Dryden; Lugari, Adrien; Hill, David E.; Grimes, Mark L.; Drubin, David. G.; Grant, Barth D.; Vidal, Marc; Boone, Charles; Sidhu, Sachdev S.; and Bader, Gary D., "SH3 Interactome Conserves General Function Over Specific Form" (2013). Biological Sciences Faculty Publications. 333.