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162 results
2023
Colin H. Lipper, Emily D. Egan, Khal-Hentz Gabriel, and Stephen C. Blacklow. 2023. “Structural Basis for Membrane-Proximal Proteolysis of Substrates by ADAM10”. Cell. doi:10.1016/j.cell.2023.06.026
Colin H. Lipper, Emily D. Egan, Khal-Hentz Gabriel, and Stephen C. Blacklow. 2023. “Structural Basis for Membrane-Proximal Proteolysis of Substrates by ADAM10”. Cell. doi:10.1016/j.cell.2023.06.026
The endopeptidase ADAM10 is a critical catalyst for the regulated proteolysis of key drivers of mammalian development, physiology, and non-amyloidogenic cleavage of APP as the primary $\alpha$-secretase. ADAM10 function requires the formation of a complex...
Wang Zheng, Shaun Rawson, Zhangfei Shen, Elakkiya Tamilselvan, Harper E. Smith, Julia Halford, Chen Shen, Swetha E. Murthy, Maximilian H. Ulbrich, Marcos Sotomayor, Tian-Min Fu, and Jeffrey R. Holt. 2023. “TMEM63 Proteins Function As Monomeric High-Threshold Mechanosensitive Ion Channels”. Neuron. doi:10.1016/j.neuron.2023.07.006
Wang Zheng, Shaun Rawson, Zhangfei Shen, Elakkiya Tamilselvan, Harper E. Smith, Julia Halford, Chen Shen, Swetha E. Murthy, Maximilian H. Ulbrich, Marcos Sotomayor, Tian-Min Fu, and Jeffrey R. Holt. 2023. “TMEM63 Proteins Function As Monomeric High-Threshold Mechanosensitive Ion Channels”. Neuron. doi:10.1016/j.neuron.2023.07.006
OSCA/TMEM63s form mechanically activated (MA) ion channels in plants and animals, respectively. OSCAs and related TMEM16s and transmembrane channel-like (TMC) proteins form homodimers with two pores. Here, we uncover an unanticipated monomeric...
Richard M. Walsh, Shaun Rawson, Helena M. Schnell, Benjamin Velez, Tamayanthi Rajakumar, and John Hanna. 2023. “Structure of the Preholoproteasome Reveals Late Steps in Proteasome Core Particle Biogenesis”. Nature Structural & Molecular Biology. doi:10.1038/s41594-023-01081-w
Richard M. Walsh, Shaun Rawson, Helena M. Schnell, Benjamin Velez, Tamayanthi Rajakumar, and John Hanna. 2023. “Structure of the Preholoproteasome Reveals Late Steps in Proteasome Core Particle Biogenesis”. Nature Structural & Molecular Biology. doi:10.1038/s41594-023-01081-w
Assembly of the proteasome's core particle (CP), a barrel-shaped chamber of four stacked rings, requires five chaperones and five subunit propeptides. Fusion of two half-CP precursors yields a complete structure but remains immature until active site...
Eun Young Park, Shaun Rawson, Anna Schmoker, Byeong-Won Kim, Sehee Oh, KangKang Song, Hyesung Jeon, and Michael J. Eck. 2023. “Cryo-EM Structure of a RAS RAF Recruitment Complex”. Nature Communications, 14, 1, Pp. 4580. doi:10.1038/s41467-023-40299-6
Eun Young Park, Shaun Rawson, Anna Schmoker, Byeong-Won Kim, Sehee Oh, KangKang Song, Hyesung Jeon, and Michael J. Eck. 2023. “Cryo-EM Structure of a RAS RAF Recruitment Complex”. Nature Communications, 14, 1, Pp. 4580. doi:10.1038/s41467-023-40299-6
RAF-family kinases are activated by recruitment to the plasma membrane by GTP-bound RAS, whereupon they initiate signaling through the MAP kinase cascade. Prior structural studies of KRAS with RAF have focused on the isolated RAS-binding and cysteine-rich...
Jun Zhang, Weichun Tang, Hailong Gao, Christy L. Lavine, Wei Shi, Hanqin Peng, Haisun Zhu, Krishna Anand, Matina Kosikova, Hyung Joon Kwon, Pei Tong, Avneesh Gautam, Sophia Rits-Volloch, Shaowei Wang, Megan L. Mayer, Duane R. Wesemann, Michael S. Seaman, Jianming Lu, Tianshu Xiao, Hang Xie, and Bing Chen. 2023. “Structural and Functional Characteristics of the SARS-CoV-2 Omicron Subvariant BA.2 Spike Protein”. Nature Structural & Molecular Biology, 30, 7, Pp. 980-90. doi:10.1038/s41594-023-01023-6
Jun Zhang, Weichun Tang, Hailong Gao, Christy L. Lavine, Wei Shi, Hanqin Peng, Haisun Zhu, Krishna Anand, Matina Kosikova, Hyung Joon Kwon, Pei Tong, Avneesh Gautam, Sophia Rits-Volloch, Shaowei Wang, Megan L. Mayer, Duane R. Wesemann, Michael S. Seaman, Jianming Lu, Tianshu Xiao, Hang Xie, and Bing Chen. 2023. “Structural and Functional Characteristics of the SARS-CoV-2 Omicron Subvariant BA.2 Spike Protein”. Nature Structural & Molecular Biology, 30, 7, Pp. 980-90. doi:10.1038/s41594-023-01023-6
The Omicron subvariant BA.2 has become the dominant circulating strain of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in many countries. Here, we have characterized structural, functional and antigenic properties of the full-length BA.2...
Wei Shi, Yongfei Cai, Haisun Zhu, Hanqin Peng, Jewel Voyer, Sophia Rits-Volloch, Hong Cao, Megan L. Mayer, KangKang Song, Chen Xu, Jianming Lu, Jun Zhang, and Bing Chen. 2023. “Cryo-EM Structure of SARS-CoV-2 Postfusion Spike in Membrane”. Nature, 619, 7969, Pp. 403-9. doi:10.1038/s41586-023-06273-4
Wei Shi, Yongfei Cai, Haisun Zhu, Hanqin Peng, Jewel Voyer, Sophia Rits-Volloch, Hong Cao, Megan L. Mayer, KangKang Song, Chen Xu, Jianming Lu, Jun Zhang, and Bing Chen. 2023. “Cryo-EM Structure of SARS-CoV-2 Postfusion Spike in Membrane”. Nature, 619, 7969, Pp. 403-9. doi:10.1038/s41586-023-06273-4
The entry of SARS-CoV-2 into host cells depends on the refolding of the virus-encoded spike protein from a prefusion conformation, which is metastable after cleavage, to a lower-energy stable postfusion conformation1,2. This transition overcomes kinetic...
Travis Walton, Miao Gui, Simona Velkova, Mahmoud R. Fassad, Robert A. Hirst, Eric Haarman, Christopher O’Callaghan, Mathieu Bottier, Thomas Burgoyne, Hannah M. Mitchison, and Alan Brown. 2023. “Axonemal Structures Reveal Mechanoregulatory and Disease Mechanisms”. Nature, 618, 7965, Pp. 625-33. doi:10.1038/s41586-023-06140-2
Travis Walton, Miao Gui, Simona Velkova, Mahmoud R. Fassad, Robert A. Hirst, Eric Haarman, Christopher O’Callaghan, Mathieu Bottier, Thomas Burgoyne, Hannah M. Mitchison, and Alan Brown. 2023. “Axonemal Structures Reveal Mechanoregulatory and Disease Mechanisms”. Nature, 618, 7965, Pp. 625-33. doi:10.1038/s41586-023-06140-2
Motile cilia and flagella beat rhythmically on the surface of cells to power the flow of fluid and to enable spermatozoa and unicellular eukaryotes to swim. In humans, defective ciliary motility can lead to male infertility and a congenital disorder...
Irina Shlosman, Elayne M. Fivenson, Morgan S.A. Gilman, Tyler A. Sisley, Suzanne Walker, Thomas G. Bernhardt, Andrew C. Kruse, and Joseph J. Loparo. 2023. “Allosteric Activation of Cell Wall Synthesis During Bacterial Growth”. Nature Communications, 14, 1, Pp. 3439. doi:10.1038/s41467-023-39037-9
Irina Shlosman, Elayne M. Fivenson, Morgan S.A. Gilman, Tyler A. Sisley, Suzanne Walker, Thomas G. Bernhardt, Andrew C. Kruse, and Joseph J. Loparo. 2023. “Allosteric Activation of Cell Wall Synthesis During Bacterial Growth”. Nature Communications, 14, 1, Pp. 3439. doi:10.1038/s41467-023-39037-9
The peptidoglycan (PG) cell wall protects bacteria against osmotic lysis and determines cell shape, making this structure a key antibiotic target. Peptidoglycan is a polymer of glycan chains connected by peptide crosslinks, and its synthesis requires...
Daniel T. D. Jones, Andrew N. Dates, Shaun D. Rawson, Maggie M. Burruss, Colin H. Lipper, and Stephen C. Blacklow. 2023. “Tethered Agonist Activated ADGRF1 Structure and Signalling Analysis Reveal Basis for G Protein Coupling”. Nature Communications, 14, 1, Pp. 2490. doi:10.1038/s41467-023-38083-7
Daniel T. D. Jones, Andrew N. Dates, Shaun D. Rawson, Maggie M. Burruss, Colin H. Lipper, and Stephen C. Blacklow. 2023. “Tethered Agonist Activated ADGRF1 Structure and Signalling Analysis Reveal Basis for G Protein Coupling”. Nature Communications, 14, 1, Pp. 2490. doi:10.1038/s41467-023-38083-7
Adhesion G Protein Coupled Receptors (aGPCRs) have evolved an activation mechanism to translate extracellular force into liberation of a tethered agonist (TA) to effect cell signalling. We report here that ADGRF1 can signal through all major G protein...
Jiazhi Li, Longfei Wang, Quentin Hahn, Radosław P. Nowak, Thibault Viennet, Esteban A. Orellana, Shourya S. Roy Burman, Hong Yue, Moritz Hunkeler, Pietro Fontana, Hao Wu, Haribabu Arthanari, Eric S. Fischer, and Richard I. Gregory. 2023. “Structural Basis of Regulated M7G TRNA Modification by METTL1–WDR4”. Nature, 613, 7943, Pp. 391-97. doi:10.1038/s41586-022-05566-4
Jiazhi Li, Longfei Wang, Quentin Hahn, Radosław P. Nowak, Thibault Viennet, Esteban A. Orellana, Shourya S. Roy Burman, Hong Yue, Moritz Hunkeler, Pietro Fontana, Hao Wu, Haribabu Arthanari, Eric S. Fischer, and Richard I. Gregory. 2023. “Structural Basis of Regulated M7G TRNA Modification by METTL1–WDR4”. Nature, 613, 7943, Pp. 391-97. doi:10.1038/s41586-022-05566-4
Chemical modifications of RNA have key roles in many biological processes1–3. N7-methylguanosine (m7G) is required for integrity and stability of a large subset of tRNAs4–7. The methyltransferase 1–WD repeat-containing protein 4 (METTL1–WDR4) complex is...
Moritz Hunkeler, Cyrus Y. Jin, and Eric S. Fischer. 2023. “Structures of BIRC6-Client Complexes Provide a Mechanism of Smac-Mediated Release of Caspases”. Science, Pp. eade5750. doi:10.1126/science.ade5750
Moritz Hunkeler, Cyrus Y. Jin, and Eric S. Fischer. 2023. “Structures of BIRC6-Client Complexes Provide a Mechanism of Smac-Mediated Release of Caspases”. Science, Pp. eade5750. doi:10.1126/science.ade5750
Tight regulation of apoptosis is essential for metazoan development and prevents diseases such as cancer and neurodegeneration. Caspase activation is central to apoptosis and inhibitor of apoptosis (IAP) proteins are the principal actors that restrain...
Brianna Duncan-Lowey, Nitzan Tal, Alex G. Johnson, Shaun Rawson, Megan L. Mayer, Shany Doron, Adi Millman, Sarah Melamed, Taya Fedorenko, Assaf Kacen, Alexander Brandis, Tevie Mehlman, Gil Amitai, Rotem Sorek, and Philip J. Kranzusch. 2023. “Cryo-EM Structure of the RADAR Supramolecular Anti-Phage Defense Complex”. Cell. doi:https://doi.org/10.1016/j.cell.2023.01.012
Brianna Duncan-Lowey, Nitzan Tal, Alex G. Johnson, Shaun Rawson, Megan L. Mayer, Shany Doron, Adi Millman, Sarah Melamed, Taya Fedorenko, Assaf Kacen, Alexander Brandis, Tevie Mehlman, Gil Amitai, Rotem Sorek, and Philip J. Kranzusch. 2023. “Cryo-EM Structure of the RADAR Supramolecular Anti-Phage Defense Complex”. Cell. doi:https://doi.org/10.1016/j.cell.2023.01.012
Summary RADAR is a two-protein bacterial defense system that was reported to defend against phage by “editing” messenger RNA. Here, we determine cryo-EM structures of the RADAR defense complex, revealing RdrA as a heptameric, two-layered AAA+ ATPase and...