Molecular Systems Biology (Jan 2013)
SH3 interactome conserves general function over specific form
- Xiaofeng Xin,
- David Gfeller,
- Jackie Cheng,
- Raffi Tonikian,
- Lin Sun,
- Ailan Guo,
- Lianet Lopez,
- Alevtina Pavlenco,
- Adenrele Akintobi,
- Yingnan Zhang,
- Jean‐François Rual,
- Bridget Currell,
- Somasekar Seshagiri,
- Tong Hao,
- Xinping Yang,
- Yun A Shen,
- Kourosh Salehi‐Ashtiani,
- Jingjing Li,
- Aaron T Cheng,
- Dryden Bouamalay,
- Adrien Lugari,
- David E Hill,
- Mark L Grimes,
- David G Drubin,
- Barth D Grant,
- Marc Vidal,
- Charles Boone,
- Sachdev S Sidhu,
- Gary D Bader
Affiliations
- Xiaofeng Xin
- The Donnelly Centre, University of Toronto Toronto Ontario Canada
- David Gfeller
- The Donnelly Centre, University of Toronto Toronto Ontario Canada
- Jackie Cheng
- Department of Molecular and Cell Biology, University of California Berkeley Berkeley CA USA
- Raffi Tonikian
- The Donnelly Centre, University of Toronto Toronto Ontario Canada
- Lin Sun
- Department of Molecular Biology and Biochemistry, Rutgers University Piscataway NJ USA
- Ailan Guo
- Cell Signaling Technology Danvers MA USA
- Lianet Lopez
- The Donnelly Centre, University of Toronto Toronto Ontario Canada
- Alevtina Pavlenco
- The Donnelly Centre, University of Toronto Toronto Ontario Canada
- Adenrele Akintobi
- Department of Molecular Biology and Biochemistry, Rutgers University Piscataway NJ USA
- Yingnan Zhang
- Department of Early Discovery Biochemistry, Genentech South San Francisco CA USA
- Jean‐François Rual
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute Boston MA USA
- Bridget Currell
- Department of Molecular Biology, Genentech South San Francisco CA USA
- Somasekar Seshagiri
- Department of Molecular Biology, Genentech South San Francisco CA USA
- Tong Hao
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute Boston MA USA
- Xinping Yang
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute Boston MA USA
- Yun A Shen
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute Boston MA USA
- Kourosh Salehi‐Ashtiani
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute Boston MA USA
- Jingjing Li
- The Donnelly Centre, University of Toronto Toronto Ontario Canada
- Aaron T Cheng
- Department of Molecular and Cell Biology, University of California Berkeley Berkeley CA USA
- Dryden Bouamalay
- Department of Molecular and Cell Biology, University of California Berkeley Berkeley CA USA
- Adrien Lugari
- IMR Laboratory, UPR 3243, Institut de Microbiologie de la Méditérannée, CNRS and Aix‐Marseille Université Marseille Cedex 20 France
- David E Hill
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute Boston MA USA
- Mark L Grimes
- Division of Biological Sciences, Center for Structural and Functional Neuroscience, The University of Montana Missoula MT USA
- David G Drubin
- Department of Molecular and Cell Biology, University of California Berkeley Berkeley CA USA
- Barth D Grant
- Department of Molecular Biology and Biochemistry, Rutgers University Piscataway NJ USA
- Marc Vidal
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute Boston MA USA
- Charles Boone
- The Donnelly Centre, University of Toronto Toronto Ontario Canada
- Sachdev S Sidhu
- The Donnelly Centre, University of Toronto Toronto Ontario Canada
- Gary D Bader
- The Donnelly Centre, University of Toronto Toronto Ontario Canada
- DOI
- https://doi.org/10.1038/msb.2013.9
- Journal volume & issue
-
Vol. 9,
no. 1
pp. n/a – n/a
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.
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