Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening

Systematic identification of direct protein-protein interactions is often hampered by difficulties in expressing and purifying the corresponding full-length proteins. By taking advantage of the modular nature of many regulatory proteins, we attempted to simplify protein-protein interactions to the c...

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Veröffentlicht in:Proteomics (Weinheim) 2007-06, Vol.7 (11), p.1775-1785
Hauptverfasser: Wu, Chenggang, Ma, Mike Haiting, Brown, Kevin R, Geisler, Matt, Li, Lei, Tzeng, Eve, Jia, Christina Y.H, Jurisica, Igor, Li, Shawn S.-C
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container_end_page 1785
container_issue 11
container_start_page 1775
container_title Proteomics (Weinheim)
container_volume 7
creator Wu, Chenggang
Ma, Mike Haiting
Brown, Kevin R
Geisler, Matt
Li, Lei
Tzeng, Eve
Jia, Christina Y.H
Jurisica, Igor
Li, Shawn S.-C
description Systematic identification of direct protein-protein interactions is often hampered by difficulties in expressing and purifying the corresponding full-length proteins. By taking advantage of the modular nature of many regulatory proteins, we attempted to simplify protein-protein interactions to the corresponding domain-ligand recognition and employed peptide arrays to identify such binding events. A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array composed of 1536 potential ligands, which led to the identification of 921 binary interactions between these proteins and 284 targets. To assess the efficiency of the peptide array target screening (PATS) method in identifying authentic protein-protein interactions, we examined a set of interactions mediated by the PLCγ1 SH3 domain by coimmunoprecipitation and/or affinity pull-downs using full-length proteins and achieved a 75% success rate. Furthermore, we characterized a novel interaction between PLCγ1 and hematopoietic progenitor kinase 1 (HPK1) identified by PATS and demonstrated that the PLCγ1 SH3 domain negatively regulated HPK1 kinase activity. Compared to protein interactions listed in the online predicted human interaction protein database (OPHID), the majority of interactions identified by PATS are novel, suggesting that, when extended to the large number of peptide interaction domains encoded by the human genome, PATS should aid in the mapping of the human interactome.
doi_str_mv 10.1002/pmic.200601006
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Furthermore, we characterized a novel interaction between PLCγ1 and hematopoietic progenitor kinase 1 (HPK1) identified by PATS and demonstrated that the PLCγ1 SH3 domain negatively regulated HPK1 kinase activity. Compared to protein interactions listed in the online predicted human interaction protein database (OPHID), the majority of interactions identified by PATS are novel, suggesting that, when extended to the large number of peptide interaction domains encoded by the human genome, PATS should aid in the mapping of the human interactome.</abstract><cop>Weinheim</cop><pub>Wiley-VCH Verlag</pub><pmid>17474147</pmid><doi>10.1002/pmic.200601006</doi><tpages>11</tpages></addata></record>
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subjects Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Binding Sites
Biological and medical sciences
Cell Line
Cells, Cultured
Fundamental and applied biological sciences. Psychology
HPK1
Humans
Interactome
Ligands
Miscellaneous
Molecular Sequence Data
Peptide array
Peptides - analysis
Peptides - metabolism
Phospholipase C gamma - metabolism
PLCγ1
Protein Array Analysis - methods
Protein Binding
Protein-Serine-Threonine Kinases - metabolism
Proteins
SH3 domain
Signal Transduction
src Homology Domains - physiology
title Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening
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