SH3 interactome conserves general function over specific form
Name
Xin-2013-SH3 interactome cons.pdf
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2.32 MB
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Checksum (MD5)
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Author(s)
Xin, Xiaofeng
Gfeller, David
Cheng, Jackie
Tonikian, Raffi
Sun, Lin
Guo, Ailan
Lopez, Lianet
Pavlenco, Alevtina
Akintobi, Adenrele
Zhang, Yingnan
Date Issued
April 2013
Journal
Molecular Systems Biology
Publisher
Nature Publishing Group
Citation
Xin, Xiaofeng, David Gfeller, Jackie Cheng, Raffi Tonikian, Lin Sun, Ailan Guo, Lianet Lopez, et al. “SH3 interactome conserves general function over specific form.” Molecular Systems Biology 9 (April 2, 2013). © 2013 EMBO and Macmillan Publishers Limited
Version
Final published version
Abstract
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 worm SH3 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.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Terms of Use
Creative Commons Attribution 3.0
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DOI of Published Version
https://doi.org/10.1038/msb.2013.9
