Phosphotyrosine interactome of the ErbB‐receptor kinase family
Open accessAbstract
Interactions between short modified peptide motifs and modular protein domains are central events in cell signal-transduction. We determined interaction partners to all cytosolic tyrosine residues of the four members of the ErbB-receptor family in an unbiased fashion by quantitative proteomics using pull-down experiments with pairs of phosphorylated and nonphosphorylated synthetic peptides. Each receptor had characteristic preferences for interacting proteins and most interaction partners had multiple binding sites on each receptor. EGFR and ErbB4 had several docking sites for Grb2, while ErbB3 was characterized by six binding sites for PI3K. We identified STAT5 as a direct binding partner to EGFR and ErbB4 and discovered new recognition motifs for Shc and STAT5. The overall pattern of interaction partners of EGFR and ErbB4 suggests similar roles during signaling through their respective ligands. Phosphorylation kinetics of several tyrosine resides was measured by mass spectrometry and correlated with interaction partner preference. Our results demonstrate that system-wide mapping of peptide-protein interactions sites is possible, and suggest shared and unique roles of ErbB-receptor family members in downstream signaling.
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The two-state approximation is likely to break down under some conditions.
“However, the assumption is likely to break down under some conditions (Schulze et al, 2005).”
From Input–output behavior of ErbB signaling pathways as revealed by a mass action model trained against dynamic data (2009) · cites this paper as Schulze et al, 2005
ErbB1 has at least 20 tyrosine phosphorylation sites on its cytoplasmic tail, 12 of which are thought to partner with SH2-containing adapter proteins and enzymes.
“ErbB1 has at least 20 sites of tyrosine phosphorylation on its cytoplasmic tail, 12 of which are thought to partner with SH2-containing adapter proteins and enzymes (Schulze et al, 2005).”
From Input–output behavior of ErbB signaling pathways as revealed by a mass action model trained against dynamic data (2009) · cites this paper as Schulze et al, 2005
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- Authors
- Schulze, W. X., Deng, L., & Mann, M.
- Affiliations
- University of Southern Denmark (DK)
- Corresponding author
- Mann, Matthias
- Venue
- Molecular Systems Biology
- Published
- 2005-05-25
- Volume
- 1
- Issue
- 1
- Pages
- 2005.0008-2005.0008
- ISSN
- 1744-4292 (ISSN-L)
- PMC
- PMC1681463
- OpenAlex
- W2125947965
- Cited by
- 753
- References
- 65
- Citations by year
- 2026: 6 · 2025: 17 · 2024: 21 · 2023: 22 · 2022: 20 · 2021: 29 · 2020: 25 · 2019: 17 · 2018: 31 · 2017: 29 · 2016: 35 · 2015: 25 · 2014: 47 · 2013: 55 · 2012: 48
- FWCI
- 25.00
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular Systems Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- University of Southern Denmark Research Portal (University of Southern Denmark) (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- European Commission
- National Research Foundation
- Danmarks Grundforskningsfond
- Topics
- Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Keywords
- ErbB receptor family, EGFR, ErbB4, HER3, receptor tyrosine kinase signaling, Grb2, phosphatidylinositol 3-kinase, STAT5, Shc, protein-peptide interactions, phosphorylation kinetics, docking site, signal transduction
- MeSH terms
- Src Homology 2 Domain-Containing, Transforming Protein 1, Amino Acid Sequence, Binding Sites, HeLa Cells, Humans, Molecular Sequence Data, Peptide Fragments, Phosphorylation, Protein Binding, Protein Processing, Post-Translational, Signal Transduction, Sequence Alignment, Protein Structure, Tertiary, Receptor, ErbB-2, Erb-b2 Receptor Tyrosine Kinases, Phosphotyrosine, Phosphatidylinositol 3-Kinases, Amino Acid Motifs, Receptor, ErbB-3, Tumor Suppressor Proteins, Protein Interaction Mapping, Immunoprecipitation, Adaptor Proteins, Signal Transducing, Systems Biology, STAT5 Transcription Factor, GRB2 Adaptor Protein, Shc Signaling Adaptor Proteins, ErbB Receptors, Receptor, ErbB-4
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