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Uncovering post-translational modification-associated protein–protein interactions
Open accessAbstract
In living systems, the chemical space and functional repertoire of proteins are dramatically expanded through the post-translational modification (PTM) of various amino acid residues. These modifications frequently trigger unique protein-protein interactions (PPIs) - for example with reader proteins that directly bind the modified amino acid residue - which leads to downstream functional outcomes. The modification of a protein can also perturb its PPI network indirectly, for example, through altering its conformation or subcellular localization. Uncovering the network of unique PTM-triggered PPIs is essential to fully understand the roles of an ever-expanding list of PTMs in our biology. In this review, we discuss established strategies and current challenges associated with this endeavor.
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“PPIs are highly specific (especially PPIs dependent on acetylated isoforms [17]) and are thus attractive, albeit challenging, therapeutic targets[18].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [17]
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Histone Recognition and Large-Scale Structural Analysis of the Human Bromodomain Family
Filippakopoulos, P., Picaud, S., Mangos, M., Keates, T., Lambert, J., Baršytė-Lovejoy, D., Felletár, I., Volkmer, R., Müller, S., Pawson, T. J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.02.013 · Cited by 1,759
Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications
Walsh, C. T., Garneau‐Tsodikova, S., & Gatto, G. J. J. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200501023 · Cited by 1,654
ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect
Yang, W., Zheng, Y., Xia, Y., Ji, H., Chen, X., Guo, F., Lyssiotis, C. A., Aldape, K., Cantley, L. C., & Lu, Z. (2012) · Nature Cell Biology · doi:10.1038/ncb2629 · Cited by 926
Post-translational modifications in signal integration
Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876
Vermeulen, M., Eberl, H. C., Matarese, F., Marks, H., Denissov, S., Butter, F., Lee, K. K., Olsen, J. V., Hyman, A. A., Stunnenberg, H. G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.020 · Cited by 806
Richter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523926113 · Cited by 755
Expanding and reprogramming the genetic code
Chin, J. W. (2017) · Nature · doi:10.1038/nature24031 · Cited by 740
Systematic Discovery of In Vivo Phosphorylation Networks
Linding, R., Jensen, L. J., Ostheimer, G. J., van Vugt, M. A. T. M., Jørgensen, C., Miron, I. M., Diella, F., Colwill, K., Taylor, L., Elder, K., et al. (2007) · Cell · doi:10.1016/j.cell.2007.05.052 · Cited by 739
Reading protein modifications with interaction domains
Seet, B. T., Đikić, I., Zhou, M., & Pawson, T. J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1960 · Cited by 665
Native Chemical Ligation and Extended Methods: Mechanisms, Catalysis, Scope, and Limitations
Agouridas, V., Mahdi, O. E., Diemer, V., Cargoët, M., Monbaliu, J. M., & Melnyk, O. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00712 · Cited by 656
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Ho, C., Chu, Y.-W., Huang, L.-Y., & Chen, C.-W. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.03.005 · Cited by 1
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Hu, X., Manini, D. R., Liu, J., Li, Y., Ying-qing, L., & Gao, Q. (2023) · Research Square · doi:10.21203/rs.3.rs-2992334/v1
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Tan, J., Wang, M., Huang, K., Xie, M., Zheng, Y., Luo, J., Tang, J., Zhai, X., He, Q., & Zhao, J. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02683-9
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Gan, D., Zeng, J., Lin, J., Chen, X., Huang, M., Weng, D., & Yan, J. (2026) · Japanese Journal of Clinical Oncology · doi:10.1093/jjco/hyag111
Zhou, J., Zhang, J., Zheng, S., Zhu, J., Wang, K., & Guo, X. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113366
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Jia, C., Ma, C., Jiang, Y., Ma, X., Yue, S., & Jianyu, J. S. (2026) · Microbiological Research · doi:10.1016/j.micres.2026.128669
Oh, Y. H., Cooke, A., Soni, H., Liu, S., Bah, M., Bellis, B., Smith, L., Capaldi, M., Levy, N., Wilhelm, E., et al. (2026) · Biotechnology and Bioengineering · doi:10.1002/bit.70321
Jiang, H., 童炜来, Wang, S., Xiong, X., Yao, G., Yang, F., Xu, Y., Liu, J., Xie, X., & Liu, Z. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06396-7
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Yangfan, L. I., Li, F., Fu, X., Zhang, X., & Ahmed, Z. F. R. (2026) · Horticultural Plant Journal · doi:10.1016/j.hpj.2026.07.001
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Altahla, R., Wang, Z., Rong, S., Li, C., Jadgal, N., Mehran, M. J., Bolideei, M., & Alshorman, J. (2026) · Clinical and Translational Discovery · doi:10.1002/ctd2.70223
Metadata
- Authors
- Wang, S., Osgood, A. O., & Chatterjee, A.
- Affiliations
- Boston College (US)
- Corresponding author
- Chatterjee, Abhishek
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2022-06
- Volume
- 74
- Pages
- 102352
- ISSN
- 0959-440X (ISSN-L)
- PMC
- PMC9464464
- OpenAlex
- W4220699331
- Cited by
- 153
- References
- 87
- Citations by year
- 2026: 44 · 2025: 54 · 2024: 28 · 2023: 24 · 2022: 3
- FWCI
- 3.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (am, 294 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Current Opinion in Structural Biology (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R35GM136437)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- post-translational modification, protein-protein interaction, protein-protein interaction network, protein conformation, subcellular localization
- MeSH terms
- Amino Acids, Protein Processing, Post-Translational, Proteins
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