Bibliographic Details
| Title: |
Proximity labeling reveals dynamic changes in the SQSTM1 protein network. |
| Authors: |
Rondón-Ortiz, Alejandro N.1,2,3, Lushuang Zhang3, Ash, Peter E. A.3, Basu, Avik2,4,5, Puri, Sambhavi3, van der Spek, Sophie J. F.3, Zihan Wang3, Dorrian, Luke3, Emili, Andrew2,4,5 emili@ohsu.edu, Wolozin, Benjamin3,6,7,8,9 bwolozin@bu.edu |
| Source: |
Journal of Biological Chemistry. Sep2024, Vol. 300 Issue 9, p1-15. 15p. |
| Subject Terms: |
*CHIMERIC proteins, *PROTEIN-protein interactions, *DISEASE progression, *CELL physiology, *CYTOLOGY |
| Abstract: |
Sequestosome1 (SQSTM1) is an autophagy receptor that mediates the degradation of intracellular cargo, including protein aggregates, through multiple protein interactions. These interactions form the SQSTM1 protein network, and these interactions are mediated by SQSTM1 functional interaction domains, which include LIR, PB1, UBA, and KIR. Technological advances in cell biology continue to expand our knowledge of the SQSTM1 protein network and the relationship between the actions of the SQSTM1 protein network in cellular physiology and disease states. Here we apply proximity profile labeling to investigate the SQSTM1 protein interaction network by fusing TurboID with the human protein SQSTM1 (TurboID::SQSTM1). This chimeric protein displayed wellestablished SQSTM1 features including production of SQSTM1 intracellular bodies, binding to known SQSTM1 interacting partners, and capture of novel SQSTM1 protein interactors. Strikingly, aggregated tau protein altered the protein interaction network of SQSTM1 to include many stressassociated proteins. We demonstrate the importance of the PB1 and/or UBA domains for binding network members, including the K18 domain of tau. Overall, our work reveals the dynamic landscape of the SQSTM1 protein network and offers a resource to study SQSTM1 function in cellular physiology and disease state. [ABSTRACT FROM AUTHOR] |
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| Database: |
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