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SH3 interactome conserves general function over specific form

delete2013-04-02
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OA
AI
X
Xiaofeng Xin
D
David Gfeller
J
Jackie Cheng
R
Raffi Tonikian
L
Lin Sun
A
Ailan Guo
A
Alevtina Pavlenco
张英楠 (Yingnan Zhang)
J
Jean‐François Rual
S
Somasekar Seshagiri
T
Tong Hao
X
Xinping Yang
Y
Yun Shen
K
Kourosh Salehi‐Ashtiani
李晶晶 封面图
李晶晶 (Jingjing Li)
A
Aaron Cheng
A
Adrien Lugari
D
David E. Hill
M
Mark L. Grimes
D
David G. Drubin
B
Barth D. Grant
M
Marc Vidal
C
Charles Boone *
S
Sachdev S. Sidhu
G
Gary D. Bader
DOI:10.1038/msb.2013.9delete
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摘要

摘要

En 中文
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.
Keyword:
network evolution
phage display
protein interaction conservation
SH3 domains
yeast two-hybrid

期刊

Molecular Systems Biology 封面图
Molecular Systems Biology
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7.7
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1.6K
被引数:
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C
cell signaling technology
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210
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Harvard University
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Dana-Farber Cancer Institute
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University of California Berkeley
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rutgers university new brunswick
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rutgers university system
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University of California System
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university of toronto
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