Molecular Systems Biology (Apr 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
- David Gfeller
- The Donnelly Centre, University of Toronto
- Jackie Cheng
- Department of Molecular and Cell Biology, University of California Berkeley
- Raffi Tonikian
- The Donnelly Centre, University of Toronto
- Lin Sun
- Department of Molecular Biology and Biochemistry, Rutgers University
- Ailan Guo
- Cell Signaling Technology
- Lianet Lopez
- The Donnelly Centre, University of Toronto
- Alevtina Pavlenco
- The Donnelly Centre, University of Toronto
- Adenrele Akintobi
- Department of Molecular Biology and Biochemistry, Rutgers University
- Yingnan Zhang
- Department of Early Discovery Biochemistry, Genentech
- Jean‐François Rual
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute
- Bridget Currell
- Department of Molecular Biology, Genentech
- Somasekar Seshagiri
- Department of Molecular Biology, Genentech
- Tong Hao
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute
- Xinping Yang
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute
- Yun A Shen
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute
- Kourosh Salehi‐Ashtiani
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute
- Jingjing Li
- The Donnelly Centre, University of Toronto
- Aaron T Cheng
- Department of Molecular and Cell Biology, University of California Berkeley
- Dryden Bouamalay
- Department of Molecular and Cell Biology, University of California Berkeley
- Adrien Lugari
- IMR Laboratory, UPR 3243, Institut de Microbiologie de la Méditérannée, CNRS and Aix‐Marseille Université
- David E Hill
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute
- Mark L Grimes
- Division of Biological Sciences, Center for Structural and Functional Neuroscience, The University of Montana
- David G Drubin
- Department of Molecular and Cell Biology, University of California Berkeley
- Barth D Grant
- Department of Molecular Biology and Biochemistry, Rutgers University
- Marc Vidal
- Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana‐Farber Cancer Institute
- Charles Boone
- The Donnelly Centre, University of Toronto
- Sachdev S Sidhu
- The Donnelly Centre, University of Toronto
- Gary D Bader
- The Donnelly Centre, University of Toronto
- DOI
- https://doi.org/10.1038/msb.2013.9
- Journal volume & issue
-
Vol. 9,
no. 1
pp. 1 – 17
Abstract
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.
Keywords