Pub Date : 2025-03-18DOI: 10.1038/s41594-025-01511-x
John McCullough, Wesley I. Sundquist
Three papers show that Vipp1, a plastid ESCRT-III protein, can form sheets, spirals and regular polygons on flat membranes and tubulate the membranes within stacked rings and helices. This work provides a framework for how Vipp1 can deliver lipids for thylakoid membrane biogenesis and protect and repair the membranes during photosynthesis.
{"title":"Thylakoid membrane remodeling by VIPP1 ESCRT-III-like filaments","authors":"John McCullough, Wesley I. Sundquist","doi":"10.1038/s41594-025-01511-x","DOIUrl":"10.1038/s41594-025-01511-x","url":null,"abstract":"Three papers show that Vipp1, a plastid ESCRT-III protein, can form sheets, spirals and regular polygons on flat membranes and tubulate the membranes within stacked rings and helices. This work provides a framework for how Vipp1 can deliver lipids for thylakoid membrane biogenesis and protect and repair the membranes during photosynthesis.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 3","pages":"414-417"},"PeriodicalIF":12.5,"publicationDate":"2025-03-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143646331","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-03-03DOI: 10.1038/s41594-025-01492-x
Gary Loughran, Dmitry E. Andreev, Ilya M. Terenin, Olivier Namy, Martin Mikl, Martina M. Yordanova, C. Joel McManus, Andrew E. Firth, John F. Atkins, Christopher S. Fraser, Zoya Ignatova, Shintaro Iwasaki, Joanna Kufel, Ola Larsson, Sebastian A. Leidel, Alexander S. Mankin, Marco Mariotti, Marvin E. Tanenbaum, Ivan Topisirovic, Nora Vázquez-Laslop, Gabriela Viero, Neva Caliskan, Yiwen Chen, Patricia L. Clark, Jonathan D. Dinman, Philip J. Farabaugh, Wendy V. Gilbert, Pavel Ivanov, Jeffrey S. Kieft, Oliver Mühlemann, Matthew S. Sachs, Ivan N. Shatsky, Nahum Sonenberg, Anna-Lena Steckelberg, Anne E. Willis, Michael T. Woodside, Leos Shivaya Valasek, Sergey E. Dmitriev, Pavel V. Baranov
Dual reporters encoding two distinct proteins within the same mRNA have had a crucial role in identifying and characterizing unconventional mechanisms of eukaryotic translation. These mechanisms include initiation via internal ribosomal entry sites (IRESs), ribosomal frameshifting, stop codon readthrough and reinitiation. This design enables the expression of one reporter to be influenced by the specific mechanism under investigation, while the other reporter serves as an internal control. However, challenges arise when intervening test sequences are placed between these two reporters. Such sequences can inadvertently impact the expression or function of either reporter, independent of translation-related changes, potentially biasing the results. These effects may occur due to cryptic regulatory elements inducing or affecting transcription initiation, splicing, polyadenylation and antisense transcription as well as unpredictable effects of the translated test sequences on the stability and activity of the reporters. Unfortunately, these unintended effects may lead to misinterpretation of data and the publication of incorrect conclusions in the scientific literature. To address this issue and to assist the scientific community in accurately interpreting dual-reporter experiments, we have developed comprehensive guidelines. These guidelines cover experimental design, interpretation and the minimal requirements for reporting results. They are designed to aid researchers conducting these experiments as well as reviewers, editors and other investigators who seek to evaluate published data. Here, the authors discuss dual-reporter systems and confounding variables that may lead to misinterpretation of results. They propose guidelines for robust design, physiological interpretation and accurate reporting when using dual reporters.
{"title":"Guidelines for minimal reporting requirements, design and interpretation of experiments involving the use of eukaryotic dual gene expression reporters (MINDR)","authors":"Gary Loughran, Dmitry E. Andreev, Ilya M. Terenin, Olivier Namy, Martin Mikl, Martina M. Yordanova, C. Joel McManus, Andrew E. Firth, John F. Atkins, Christopher S. Fraser, Zoya Ignatova, Shintaro Iwasaki, Joanna Kufel, Ola Larsson, Sebastian A. Leidel, Alexander S. Mankin, Marco Mariotti, Marvin E. Tanenbaum, Ivan Topisirovic, Nora Vázquez-Laslop, Gabriela Viero, Neva Caliskan, Yiwen Chen, Patricia L. Clark, Jonathan D. Dinman, Philip J. Farabaugh, Wendy V. Gilbert, Pavel Ivanov, Jeffrey S. Kieft, Oliver Mühlemann, Matthew S. Sachs, Ivan N. Shatsky, Nahum Sonenberg, Anna-Lena Steckelberg, Anne E. Willis, Michael T. Woodside, Leos Shivaya Valasek, Sergey E. Dmitriev, Pavel V. Baranov","doi":"10.1038/s41594-025-01492-x","DOIUrl":"10.1038/s41594-025-01492-x","url":null,"abstract":"Dual reporters encoding two distinct proteins within the same mRNA have had a crucial role in identifying and characterizing unconventional mechanisms of eukaryotic translation. These mechanisms include initiation via internal ribosomal entry sites (IRESs), ribosomal frameshifting, stop codon readthrough and reinitiation. This design enables the expression of one reporter to be influenced by the specific mechanism under investigation, while the other reporter serves as an internal control. However, challenges arise when intervening test sequences are placed between these two reporters. Such sequences can inadvertently impact the expression or function of either reporter, independent of translation-related changes, potentially biasing the results. These effects may occur due to cryptic regulatory elements inducing or affecting transcription initiation, splicing, polyadenylation and antisense transcription as well as unpredictable effects of the translated test sequences on the stability and activity of the reporters. Unfortunately, these unintended effects may lead to misinterpretation of data and the publication of incorrect conclusions in the scientific literature. To address this issue and to assist the scientific community in accurately interpreting dual-reporter experiments, we have developed comprehensive guidelines. These guidelines cover experimental design, interpretation and the minimal requirements for reporting results. They are designed to aid researchers conducting these experiments as well as reviewers, editors and other investigators who seek to evaluate published data. Here, the authors discuss dual-reporter systems and confounding variables that may lead to misinterpretation of results. They propose guidelines for robust design, physiological interpretation and accurate reporting when using dual reporters.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 3","pages":"418-430"},"PeriodicalIF":12.5,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143532507","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-03-03DOI: 10.1038/s41594-025-01504-w
Nicole J. Francis
The structure of chromatin bound by Polycomb repressive complex 1 (PRC1) and how it contributes to transcription repression are unknown. Here, cryo-electron tomography (cryo-ET) of PRC1–chromatin condensates reveal randomly oriented neighboring nucleosomes in a stable, open chromatin mesh that might exclude large protein complexes to repress transcription.
{"title":"A chromatin mesh model for compaction of chromatin by PRC1 in condensates","authors":"Nicole J. Francis","doi":"10.1038/s41594-025-01504-w","DOIUrl":"10.1038/s41594-025-01504-w","url":null,"abstract":"The structure of chromatin bound by Polycomb repressive complex 1 (PRC1) and how it contributes to transcription repression are unknown. Here, cryo-electron tomography (cryo-ET) of PRC1–chromatin condensates reveal randomly oriented neighboring nucleosomes in a stable, open chromatin mesh that might exclude large protein complexes to repress transcription.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 3","pages":"411-413"},"PeriodicalIF":12.5,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143532503","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-18DOI: 10.1038/s41594-025-01510-y
We discuss work at the forefront of structural cell biology featured in this issue.
{"title":"From atoms to cells","authors":"","doi":"10.1038/s41594-025-01510-y","DOIUrl":"10.1038/s41594-025-01510-y","url":null,"abstract":"We discuss work at the forefront of structural cell biology featured in this issue.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 2","pages":"213-213"},"PeriodicalIF":12.5,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.com/articles/s41594-025-01510-y.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143439259","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-14DOI: 10.1038/s41594-025-01496-7
Meng Zhang, Yaxu Wang, M. Madan Babu
The ghrelin receptor (GHSR1a) is a key target for treating cancer cachexia. A study now reveals the structure of the GHSR1a–miniGq complex bound to the approved drug anamorelin, providing insights into the role of superagonism in cancer cachexia therapy. The comprehensive study represents a framework for personalized treatment strategies.
{"title":"Personalized medicine for cancer cachexia via the ghrelin receptor","authors":"Meng Zhang, Yaxu Wang, M. Madan Babu","doi":"10.1038/s41594-025-01496-7","DOIUrl":"10.1038/s41594-025-01496-7","url":null,"abstract":"The ghrelin receptor (GHSR1a) is a key target for treating cancer cachexia. A study now reveals the structure of the GHSR1a–miniGq complex bound to the approved drug anamorelin, providing insights into the role of superagonism in cancer cachexia therapy. The comprehensive study represents a framework for personalized treatment strategies.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 3","pages":"408-410"},"PeriodicalIF":12.5,"publicationDate":"2025-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143417657","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-13DOI: 10.1038/s41594-025-01503-x
Dimitris Typas
{"title":"An in vivo platform to screen for regulators of Huntington’s disease","authors":"Dimitris Typas","doi":"10.1038/s41594-025-01503-x","DOIUrl":"10.1038/s41594-025-01503-x","url":null,"abstract":"","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 2","pages":"214-214"},"PeriodicalIF":12.5,"publicationDate":"2025-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143401324","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-02-06DOI: 10.1038/s41594-025-01487-8
Evan J. Worden
PRC2-dependent H3K27 methylation must be excluded from active genes to support appropriate transcriptional programs. Structures of PRC2 bound to nucleosome substrates containing histone modifications associated with active transcription explain how PRC2 is inhibited at active genes.
{"title":"Multiple allosteric mechanisms suppress PRC2 activity at active genes","authors":"Evan J. Worden","doi":"10.1038/s41594-025-01487-8","DOIUrl":"10.1038/s41594-025-01487-8","url":null,"abstract":"PRC2-dependent H3K27 methylation must be excluded from active genes to support appropriate transcriptional programs. Structures of PRC2 bound to nucleosome substrates containing histone modifications associated with active transcription explain how PRC2 is inhibited at active genes.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 2","pages":"215-216"},"PeriodicalIF":12.5,"publicationDate":"2025-02-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143192105","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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