Pub Date : 2025-11-24DOI: 10.1016/j.molcel.2025.11.003
Hendrik Glauninger, Jared A.M. Bard, Caitlin J. Wong Hickernell, Karen M. Velez, Edo M. Airoldi, Weihan Li, Robert H. Singer, Sneha Paul, Jingyi Fei, Tobin R. Sosnick, Edward W.J. Wallace, D. Allan Drummond
Stress-induced messenger ribonucleoprotein (mRNP) condensation is conserved across eukaryotes, resulting in stress granule formation under intense stresses, yet the mRNA composition and function of these condensates remain unclear. Exposure of ribosome-free mRNA following stress is thought to cause condensation and stress granule formation through mRNA-sequence-dependent interactions, leading to disproportionate condensation of long mRNAs. Here, we show that, by contrast, virtually all mRNAs condense in response to multiple stresses in budding yeast with minor length dependence and often without stress granule formation. New transcripts escape mRNP condensation, enabling their selective translation. Inhibiting translation initiation causes formation of mRNP condensates distinct from stress granules and processing bodies (P bodies), and these translation-initiation-inhibited condensates (TIICs) are omnipresent, even in unstressed cells. Stress-induced mRNAs are excluded from TIICs due to the timing of their expression, indicating determinants of escape that are independent of sequence. Together, our results reveal a previously undetected level of translation-linked molecular organization and stress-responsive regulation.
{"title":"Transcriptome-wide mRNP condensation precedes stress granule formation and excludes new mRNAs","authors":"Hendrik Glauninger, Jared A.M. Bard, Caitlin J. Wong Hickernell, Karen M. Velez, Edo M. Airoldi, Weihan Li, Robert H. Singer, Sneha Paul, Jingyi Fei, Tobin R. Sosnick, Edward W.J. Wallace, D. Allan Drummond","doi":"10.1016/j.molcel.2025.11.003","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.11.003","url":null,"abstract":"Stress-induced messenger ribonucleoprotein (mRNP) condensation is conserved across eukaryotes, resulting in stress granule formation under intense stresses, yet the mRNA composition and function of these condensates remain unclear. Exposure of ribosome-free mRNA following stress is thought to cause condensation and stress granule formation through mRNA-sequence-dependent interactions, leading to disproportionate condensation of long mRNAs. Here, we show that, by contrast, virtually all mRNAs condense in response to multiple stresses in budding yeast with minor length dependence and often without stress granule formation. New transcripts escape mRNP condensation, enabling their selective translation. Inhibiting translation initiation causes formation of mRNP condensates distinct from stress granules and processing bodies (P bodies), and these translation-initiation-inhibited condensates (TIICs) are omnipresent, even in unstressed cells. Stress-induced mRNAs are excluded from TIICs due to the timing of their expression, indicating determinants of escape that are independent of sequence. Together, our results reveal a previously undetected level of translation-linked molecular organization and stress-responsive regulation.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"32 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145583761","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}
Lariat RNAs, generated as byproducts of RNA splicing from excised introns, must be removed. RNA debranching enzyme (DBR1) is the core factor responsible for lariat RNA removal. However, the mechanism by which DBR1 debranches lariat RNAs remains unclear. Here, we demonstrate that six ALBA (acetylation lowers binding affinity) proteins interact with DBR1 to enhance its debranching activity and facilitate DBR1’s accessibility to lariat RNAs, thereby promoting lariat RNA turnover. Similar to dbr1, alba mutants exhibit pleiotropic developmental defects and accumulate lariat RNAs. ALBAs bind to lariat RNAs via their C-terminal Arg-Gly-Gly/Arg-Gly (RGG/RG)-rich repeats and assist DBR1 in binding to these RNAs. The N-terminal ALBA domain mediates the interaction with DBR1 and enhances its enzymatic activity. Cold stress induces lariat RNA accumulation by attenuating the ALBA-DBR1 interaction, which in turn reduces the induction of cold-responsive genes by impairing their transcription. Together, these findings uncover that lariat RNA turnover requires ALBA proteins.
{"title":"Debranching enzyme DBR1-mediated lariat RNA turnover requires ALBA proteins in Arabidopsis","authors":"Haoran Ge, Qi Tang, Jingjing Wu, Xiaotuo Zhang, Yuxuan Li, Weiqaing Qian, Jinbiao Ma, Binglian Zheng","doi":"10.1016/j.molcel.2025.10.021","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.10.021","url":null,"abstract":"Lariat RNAs, generated as byproducts of RNA splicing from excised introns, must be removed. RNA debranching enzyme (DBR1) is the core factor responsible for lariat RNA removal. However, the mechanism by which DBR1 debranches lariat RNAs remains unclear. Here, we demonstrate that six ALBA (acetylation lowers binding affinity) proteins interact with DBR1 to enhance its debranching activity and facilitate DBR1’s accessibility to lariat RNAs, thereby promoting lariat RNA turnover. Similar to <em>dbr1</em>, <em>alba</em> mutants exhibit pleiotropic developmental defects and accumulate lariat RNAs. ALBAs bind to lariat RNAs via their C-terminal Arg-Gly-Gly/Arg-Gly (RGG/RG)-rich repeats and assist DBR1 in binding to these RNAs. The N-terminal ALBA domain mediates the interaction with DBR1 and enhances its enzymatic activity. Cold stress induces lariat RNA accumulation by attenuating the ALBA-DBR1 interaction, which in turn reduces the induction of cold-responsive genes by impairing their transcription. Together, these findings uncover that lariat RNA turnover requires ALBA proteins.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"1 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145554807","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 : 2025-11-20DOI: 10.1016/j.molcel.2025.10.027
Benjamin Le Bozec, Laure Guitton-Sert, Sarah Collins, Anne-Laure Finoux, Charlotte Payrault, Emmanuelle Guillou, Marion Aguirrebengoa, Vanessa Dougados, Virginie Jouffret, Jessica Frison, Romane Carette, Vincent Rocher, Coline Arnould, Aude Guénolé, Ikrame Lazar, Aline Marnef, Philippe Frit, Patrick Calsou, Thomas Mangeat, Nadine Puget, Gaëlle Legube
Repair of DNA double-strand breaks (DSBs) produced in transcriptionally active chromatin occurs through a poorly characterized pathway called transcription-coupled DSB repair (TC-DSBR). Here, using a screening approach scoring multiple outputs in human cells, we identified proteins from the PERIOD complex, ensuring circadian oscillations, as previously unknown TC-DSBR players. We show that PER2 is recruited at TC-DSBs and contributes to their targeting to the nuclear envelope (NE), where SUN1 and the nuclear pore complex (NPC) act as docking sites. TC-DSB anchoring at the NE fosters RAD51 assembly and prevents DSB clustering and translocations. In agreement, the circadian clock regulates TC-DSB targeting to the NE, RAD51 assembly, and DSB clustering. Our study shows a direct link between the circadian rhythm and the response to DSBs in transcribed genes, opening strategies for chrono-chemotherapies based on topoisomerase poisons that induce DSBs in active loci.
{"title":"Circadian PERIOD proteins regulate TC-DSB repair through anchoring to the nuclear envelope","authors":"Benjamin Le Bozec, Laure Guitton-Sert, Sarah Collins, Anne-Laure Finoux, Charlotte Payrault, Emmanuelle Guillou, Marion Aguirrebengoa, Vanessa Dougados, Virginie Jouffret, Jessica Frison, Romane Carette, Vincent Rocher, Coline Arnould, Aude Guénolé, Ikrame Lazar, Aline Marnef, Philippe Frit, Patrick Calsou, Thomas Mangeat, Nadine Puget, Gaëlle Legube","doi":"10.1016/j.molcel.2025.10.027","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.10.027","url":null,"abstract":"Repair of DNA double-strand breaks (DSBs) produced in transcriptionally active chromatin occurs through a poorly characterized pathway called transcription-coupled DSB repair (TC-DSBR). Here, using a screening approach scoring multiple outputs in human cells, we identified proteins from the PERIOD complex, ensuring circadian oscillations, as previously unknown TC-DSBR players. We show that PER2 is recruited at TC-DSBs and contributes to their targeting to the nuclear envelope (NE), where SUN1 and the nuclear pore complex (NPC) act as docking sites. TC-DSB anchoring at the NE fosters RAD51 assembly and prevents DSB clustering and translocations. In agreement, the circadian clock regulates TC-DSB targeting to the NE, RAD51 assembly, and DSB clustering. Our study shows a direct link between the circadian rhythm and the response to DSBs in transcribed genes, opening strategies for chrono-chemotherapies based on topoisomerase poisons that induce DSBs in active loci.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"11 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145554801","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 : 2025-11-20DOI: 10.1016/j.molcel.2025.10.030
Guodi Cai, Zhenhua Zhang, Lin Zhong, Hong Wang, Miaomiao Miao, Jingtian Su, Yana An, Chenxi Zhang, Xiaowei Luo, Huai-Qiang Ju, Jian Zhang, Wanyi Huang, Zhe Li, Peiqing Liu, Dinglan Wu, Franky Leung Chan, Huihao Zhou, Fanghai Han, Hong-Wu Chen, Tao Su, Junjian Wang
Nucleotide metabolism reprogramming drives tumor progression, yet how tumor cells sense nucleotide levels remains unclear. Here, we identified UMP as an endogenous regulator of the orphan nuclear receptor NR4A1 in gastric cancer (GCa). Under UMP sufficiency, UMP directly binds to NR4A1, inhibiting its tumor-suppressive function and promoting GCa progression. Conversely, UMP deficiency resulting from disrupted pyrimidine biosynthesis derepresses NR4A1, which suppresses GCa cell survival and progression by both increasing NR4A1 occupancy at super-enhancers to reprogram survival-gene expression and enhancing NR4A1’s pro-apoptotic activity at the mitochondria. NR4A1 loss was sufficient to rescue the effects of pyrimidine nucleotide stress on GCa cells in vitro and in vivo. NR4A1 agonists suppressed the pyrimidine salvage pathway triggered by de novo pyrimidine biosynthesis (DNPB) inhibition. Co-targeting DNPB and NR4A1 induced synergistic tumor lethality in GCa xenograft models. Together, our results establish UMP as an endogenous regulator of NR4A1 and provide an effective therapeutic strategy for GCa.
{"title":"UMP functions as an endogenous regulator of NR4A1 to control gastric cancer progression","authors":"Guodi Cai, Zhenhua Zhang, Lin Zhong, Hong Wang, Miaomiao Miao, Jingtian Su, Yana An, Chenxi Zhang, Xiaowei Luo, Huai-Qiang Ju, Jian Zhang, Wanyi Huang, Zhe Li, Peiqing Liu, Dinglan Wu, Franky Leung Chan, Huihao Zhou, Fanghai Han, Hong-Wu Chen, Tao Su, Junjian Wang","doi":"10.1016/j.molcel.2025.10.030","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.10.030","url":null,"abstract":"Nucleotide metabolism reprogramming drives tumor progression, yet how tumor cells sense nucleotide levels remains unclear. Here, we identified UMP as an endogenous regulator of the orphan nuclear receptor NR4A1 in gastric cancer (GCa). Under UMP sufficiency, UMP directly binds to NR4A1, inhibiting its tumor-suppressive function and promoting GCa progression. Conversely, UMP deficiency resulting from disrupted pyrimidine biosynthesis derepresses NR4A1, which suppresses GCa cell survival and progression by both increasing NR4A1 occupancy at super-enhancers to reprogram survival-gene expression and enhancing NR4A1’s pro-apoptotic activity at the mitochondria. NR4A1 loss was sufficient to rescue the effects of pyrimidine nucleotide stress on GCa cells <em>in vitro</em> and <em>in vivo</em>. NR4A1 agonists suppressed the pyrimidine salvage pathway triggered by <em>de novo</em> pyrimidine biosynthesis (DNPB) inhibition. Co-targeting DNPB and NR4A1 induced synergistic tumor lethality in GCa xenograft models. Together, our results establish UMP as an endogenous regulator of NR4A1 and provide an effective therapeutic strategy for GCa.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"160 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145554800","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 : 2025-11-20DOI: 10.1016/j.molcel.2025.10.032
Morris F. White
Wang et al.1 use innovative computational methods to design polypeptides that bind to and activate the insulin receptor tyrosine kinase, revealing strategies to resolve the composite insulin signal into distinct components for therapeutic use.
{"title":"A new horizon unfolding for insulin signaling in health and disease","authors":"Morris F. White","doi":"10.1016/j.molcel.2025.10.032","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.10.032","url":null,"abstract":"Wang et al.<span><span><sup>1</sup></span></span> use innovative computational methods to design polypeptides that bind to and activate the insulin receptor tyrosine kinase, revealing strategies to resolve the composite insulin signal into distinct components for therapeutic use.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"82 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145554803","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 : 2025-11-20DOI: 10.1016/j.molcel.2025.10.029
Michaela Müller-McNicoll
Recent work by Faraway et al.1 uncovers interstasis—a feedback mechanism whereby the stiffening of nuclear condensates caused by the accumulation of condensation-prone resident proteins entraps mRNAs encoding these proteins, thereby limiting their translation to restore proteome balance.
{"title":"Getting sticky: How nuclear speckles tune the condensation-prone proteome","authors":"Michaela Müller-McNicoll","doi":"10.1016/j.molcel.2025.10.029","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.10.029","url":null,"abstract":"Recent work by Faraway et al.<span><span><sup>1</sup></span></span> uncovers interstasis—a feedback mechanism whereby the stiffening of nuclear condensates caused by the accumulation of condensation-prone resident proteins entraps mRNAs encoding these proteins, thereby limiting their translation to restore proteome balance.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"41 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145554805","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 : 2025-11-20DOI: 10.1016/j.molcel.2025.10.023
Yi Di, Wenxue Li, Joan Josep Castellano, Wenjie Jin, Joanna N. Modi, Barbora Salovska, Delyar Khosroabadi, Wei Hu, Alison M. Taylor, Yansheng Liu
How aneuploid cells tolerate chromosome arm gains or losses remains an open question. Using an isogenic human lung cell model with either chromosome 3p loss or 3q gain, combined with quantitative mass spectrometry and isotopic labeling, we reveal distinct proteostasis mechanisms for gain- and loss-type aneuploidy. Surprisingly, while compensation for 3q gain is primarily driven by increased degradation of excess protein complex subunits, 3p loss is neither counteracted by global protein degradation nor selectively reduced degradation. Rather, there is a relative upregulation in protein synthesis of those 3p-encoded proteins that participate in stable protein complexes to maintain functional complex stoichiometry. Additionally, 3p-encoded proteins that are in a complex show increased thermal stability in loss-type aneuploidy, potentially via their interactions with other proteins from euploid chromosomes. Together, our findings uncover distinct proteomic buffering strategies that enable cells to tolerate either excessive or deficient single-arm aneuploidy.
{"title":"Divergent proteome tolerance against gain and loss of chromosome arms","authors":"Yi Di, Wenxue Li, Joan Josep Castellano, Wenjie Jin, Joanna N. Modi, Barbora Salovska, Delyar Khosroabadi, Wei Hu, Alison M. Taylor, Yansheng Liu","doi":"10.1016/j.molcel.2025.10.023","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.10.023","url":null,"abstract":"How aneuploid cells tolerate chromosome arm gains or losses remains an open question. Using an isogenic human lung cell model with either chromosome <em>3p loss</em> or <em>3q gain</em>, combined with quantitative mass spectrometry and isotopic labeling, we reveal distinct proteostasis mechanisms for gain- and loss-type aneuploidy. Surprisingly, while compensation for <em>3q gain</em> is primarily driven by increased degradation of excess protein complex subunits, <em>3p loss</em> is neither counteracted by global protein degradation nor selectively reduced degradation. Rather, there is a relative upregulation in protein synthesis of those 3p-encoded proteins that participate in stable protein complexes to maintain functional complex stoichiometry. Additionally, 3p-encoded proteins that are in a complex show increased thermal stability in loss-type aneuploidy, potentially via their interactions with other proteins from euploid chromosomes. Together, our findings uncover distinct proteomic buffering strategies that enable cells to tolerate either excessive or deficient single-arm aneuploidy.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"20 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145554808","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 : 2025-11-20DOI: 10.1016/j.molcel.2025.10.020
Timothy C. Kenny, Kıvanç Birsoy
In this issue of Molecular Cell, Nengroo et al.1 report that the tricarboxylic acid (TCA) cycle enzyme succinate dehydrogenase (SDH) is essential for de novo purine synthesis, revealing a previously unrecognized metabolic dependency in cancer that can be leveraged therapeutically.
{"title":"Succinate puts the brakes on de novo purine synthesis","authors":"Timothy C. Kenny, Kıvanç Birsoy","doi":"10.1016/j.molcel.2025.10.020","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.10.020","url":null,"abstract":"In this issue of <em>Molecular Cell</em>, Nengroo et al.<span><span><sup>1</sup></span></span> report that the tricarboxylic acid (TCA) cycle enzyme succinate dehydrogenase (SDH) is essential for <em>de novo</em> purine synthesis, revealing a previously unrecognized metabolic dependency in cancer that can be leveraged therapeutically.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"147 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145554855","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 : 2025-11-20DOI: 10.1016/j.molcel.2025.10.024
Daniela Barillà
Asgard archaea are widely considered the closest living relatives of eukaryotes. In this issue of Molecular Cell, Ranawat et al.1 report high-resolution structures of hypernucleosomes formed by the hodarchaeal HHoB histone, disclosing open and closed chromatin conformations.
{"title":"Let’s wrap things up: Open and closed hypernucleosomes in Asgard archaea","authors":"Daniela Barillà","doi":"10.1016/j.molcel.2025.10.024","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.10.024","url":null,"abstract":"Asgard archaea are widely considered the closest living relatives of eukaryotes. In this issue of <em>Molecular Cell</em>, Ranawat et al.<span><span><sup>1</sup></span></span> report high-resolution structures of hypernucleosomes formed by the hodarchaeal HHoB histone, disclosing open and closed chromatin conformations.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"1 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145554802","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 : 2025-11-20DOI: 10.1016/j.molcel.2025.10.031
Emeline Joulia, Christian M. Metallo
In a recent Nature article, Xiao et al.1 report development of a metabolite-protein covariation architecture (MPCA) database from a diversity outbred mouse cohort that facilitates the deciphering of metabolite-protein relationships in liver and brown adipose tissue (BAT). Using these correlations, the authors describe a role for LRRC58 in controlling cysteine-taurine metabolism.
{"title":"Leveraging biochemical covariance to better understand biology","authors":"Emeline Joulia, Christian M. Metallo","doi":"10.1016/j.molcel.2025.10.031","DOIUrl":"https://doi.org/10.1016/j.molcel.2025.10.031","url":null,"abstract":"In a recent <em>Nature</em> article, Xiao et al.<span><span><sup>1</sup></span></span> report development of a metabolite-protein covariation architecture (MPCA) database from a diversity outbred mouse cohort that facilitates the deciphering of metabolite-protein relationships in liver and brown adipose tissue (BAT). Using these correlations, the authors describe a role for LRRC58 in controlling cysteine-taurine metabolism.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"28 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145554804","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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