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dc.contributor.authorXin, Xiaofeng
dc.contributor.authorGfeller, David
dc.contributor.authorCheng, Jackie
dc.contributor.authorTonikian, Raffi
dc.contributor.authorSun, Lin
dc.contributor.authorGuo, Ailan
dc.contributor.authorLopez, Lianet
dc.contributor.authorPavlenco, Alevtina
dc.contributor.authorAkintobi, Adenrele
dc.contributor.authorZhang, Yingnan
dc.contributor.authorRual, Jean-François
dc.contributor.authorCurrell, Bridget
dc.contributor.authorSeshagiri, Somasekar
dc.contributor.authorHao, Tong
dc.contributor.authorYang, Xinping
dc.contributor.authorShen, Yun A
dc.contributor.authorSalehi-Ashtiani, Kourosh
dc.contributor.authorLi, Jingjing
dc.contributor.authorCheng, Aaron T
dc.contributor.authorBouamalay, Dryden
dc.contributor.authorLugari, Adrien
dc.contributor.authorHill, David E.
dc.contributor.authorGrimes, Mark L
dc.contributor.authorDrubin, David G
dc.contributor.authorGrant, Barth D
dc.contributor.authorVidal, Marc
dc.contributor.authorBoone, Charles
dc.contributor.authorSidhu, Sachdev S
dc.contributor.authorBader, Gary D
dc.date.accessioned2013-10-16T14:07:21Z
dc.date.issued2013
dc.identifier.citationXin, Xiaofeng, David Gfeller, Jackie Cheng, Raffi Tonikian, Lin Sun, Ailan Guo, Lianet Lopez, et al. 2013. Sh3 interactome conserves general function over specific form. Molecular Systems Biology 9: 652.en_US
dc.identifier.issn1744-4292en_US
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:11177914
dc.description.abstractSrc 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.en_US
dc.language.isoen_USen_US
dc.publisherNature Publishing Groupen_US
dc.relation.isversionofdoi:10.1038/msb.2013.9en_US
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3658277/pdf/en_US
dash.licenseLAA
dc.subjectnetwork evolutionen_US
dc.subjectphage displayen_US
dc.subjectprotein interaction conservationen_US
dc.subjectSH3 domainsen_US
dc.subjectyeast two-hybriden_US
dc.titleSH3 interactome conserves general function over specific formen_US
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden_US
dc.relation.journalMolecular Systems Biologyen_US
dash.depositing.authorVidal, Marc
dc.date.available2013-10-16T14:07:21Z
dc.identifier.doi10.1038/msb.2013.9*
dash.authorsorderedfalse
dash.contributor.affiliatedYang, Xinping
dash.contributor.affiliatedHill, David
dash.contributor.affiliatedVidal, Marc


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