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When two’s a crowd - Structural mapping of PEAK pseudokinase interactions identifies 14 3 3 as a molecular switch for PEAK3/Crk signaling.
Open accessPreprint — published as 10.1038/s41467-023-38869-9
Abstract
PEAK pseudokinases regulate cell migration, invasion and proliferation by recruiting key signaling proteins to the cytoskeleton. Despite lacking catalytic activity, alteration in their expression level is associated with several aggressive cancers. Here, we elucidate new molecular details of key PEAK signaling interactions with the adapter proteins CrkII and Grb2 and the scaffold protein 14-3-3. Our findings rationalize why the dimerization of PEAK proteins has a crucial function in signal transduction and provide biophysical and structural data to unravel binding specificity within the PEAK interactome. We identify a conserved high affinity 14-3-3 motif on PEAK3 and demonstrate its role as a molecular switch to regulate CrkII binding. Together, our studies provide a detailed structural snapshot of PEAK interaction networks and further elucidate how PEAK proteins, especially PEAK3, act as dynamic scaffolds that exploit adapter proteins to control signal transduction in cell growth/motility and cancer.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Lucet, I., Roy, M., Surudoi, M., Kropp, A., Hou, J., Dai, W., Hardy, J., Liang, L.-Y., Cotton, T., Lechtenberg, B., Dite, T., Ma, X., Daly, R., & Patel, O.
- Affiliations
- The University of Melbourne (AU)
- Monash University (AU)
- Corresponding author
- Lucet, Isabelle
- Roy, Michael
- ORCID
- Venue
- Nature Communications
- Published
- 2022-08-31
- Volume
- 14
- Issue
- 1
- Pages
- 3542-3542
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC10279719
- OpenAlex
- W4381251107
- Cited by
- 16
- References
- 1
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 5 · 2023: 2
- FWCI
- 1.42
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Australian Nuclear Science and Technology Organisation
- Australian Cancer Research Foundation
- Australian Synchrotron
- Monash University
- University of Melbourne
- State Government of Victoria (9000719)
- Department of Education and Training (DP190103672, DP220103638)
- Medical Research Council
- Australian Research Council (DP190103672, DP220103638)
- National Health and Medical Research Council (IRIISS (9000719), 1144149, 9000719, 2008096)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 14-3-3 protein interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- CrkII, Grb2, protein-protein interaction, protein dimerization, signaling scaffolds, adaptor proteins, cytoskeleton, cell migration, cancer, binding specificity, molecular switches
- MeSH terms
- Cell Movement, Cytoskeletal Proteins, Signal Transduction, 14-3-3 Proteins, Cell Proliferation
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