Cell Research最新文献

{"title":"Structure and genome editing activity of the novel CRISPR-Cas12o1 effector.","authors":"Zhiqiang Duan, Xi Zhang, Jun-Tao Zhang, Xingkun Ji, Ruiheng Liu, Ying Chen, Shanshan Li, Nannan Jia, Huizhi Gao, Yu Xin, Ning Jia, Jian-Kang Zhu","doi":"10.1038/s41422-024-01050-y","DOIUrl":"https://doi.org/10.1038/s41422-024-01050-y","url":null,"abstract":"","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":" ","pages":""},"PeriodicalIF":28.1,"publicationDate":"2024-11-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142615977","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}

{"title":"scNanoCOOL-seq: a long-read single-cell sequencing method for multi-omics profiling within individual cells","authors":"Jianli Lin, Xiaohui Xue, Yan Wang, Yuan Zhou, Jian Wu, Haoling Xie, Mengya Liu, Lu Wen, Fuchou Tang","doi":"10.1038/s41422-023-00873-5","DOIUrl":"10.1038/s41422-023-00873-5","url":null,"abstract":"","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":"33 11","pages":"879-882"},"PeriodicalIF":44.1,"publicationDate":"2023-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10214775","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}

{"title":"RHIMoving fibrils of death","authors":"Bart Tummers","doi":"10.1038/s41422-023-00875-3","DOIUrl":"10.1038/s41422-023-00875-3","url":null,"abstract":"","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":"33 11","pages":"811-812"},"PeriodicalIF":44.1,"publicationDate":"2023-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10624819/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10214773","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}

{"title":"Platelet and myeloid lineage biases of transplanted single perinatal mouse hematopoietic stem cells","authors":"Karin Belander Strålin, Joana Carrelha, Axel Winroth, Christoph Ziegenhain, Michael Hagemann-Jensen, Laura M. Kettyle, Amy Hillen, Kari Högstrand, Ellen Markljung, Francesca Grasso, Masafumi Seki, Stefania Mazzi, Yiran Meng, Bishan Wu, Edwin Chari, Madeleine Lehander, Rickard Sandberg, Petter S. Woll, Sten Eirik W. Jacobsen","doi":"10.1038/s41422-023-00866-4","DOIUrl":"10.1038/s41422-023-00866-4","url":null,"abstract":"","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":"33 11","pages":"883-886"},"PeriodicalIF":44.1,"publicationDate":"2023-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10624660/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10172949","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}

{"title":"Cryo-EM structures of human organic anion transporting polypeptide OATP1B1","authors":"Ziyang Shan, Xuemei Yang, Huihui Liu, Yafei Yuan, Yuan Xiao, Jing Nan, Wei Zhang, Wenqi Song, Jufang Wang, Feiwen Wei, Yanqing Zhang","doi":"10.1038/s41422-023-00870-8","DOIUrl":"10.1038/s41422-023-00870-8","url":null,"abstract":"Members of the solute carrier organic anion transporting polypeptide (OATPs) family function as transporters for a large variety of amphipathic organic anions including endogenous metabolites and clinical drugs, such as bile salts, steroids, thyroid hormones, statins, antibiotics, antivirals, and anticancer drugs. OATP1B1 plays a vital role in transporting such substances into the liver for hepatic clearance. FDA and EMA recommend conducting in vitro testing of drug–drug interactions (DDIs) involving OATP1B1. However, the structure and working mechanism of OATPs still remains elusive. In this study, we determined cryo-EM structures of human OATP1B1 bound with representative endogenous metabolites (bilirubin and estrone-3-sulfate), a clinical drug (simeprevir), and a fluorescent indicator (2′,7′-dichlorofluorescein), in both outward- and inward-open states. These structures reveal major and minor substrate binding pockets and conformational changes during transport. In combination with mutagenesis studies and molecular dynamics simulations, our work comprehensively elucidates the transport mechanism of OATP1B1 and provides the structural basis for DDI predictions involving OATP1B1, which will greatly promote our understanding of OATPs.","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":"33 12","pages":"940-951"},"PeriodicalIF":44.1,"publicationDate":"2023-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10709409/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10226394","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}

{"title":"Swiss army knife T cell: one T cell many tumor targets","authors":"Abdulla Berjis, Deeksha Muthumani, Neil C. Sheppard, Carl H. June","doi":"10.1038/s41422-023-00871-7","DOIUrl":"10.1038/s41422-023-00871-7","url":null,"abstract":"","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":"34 1","pages":"5-6"},"PeriodicalIF":44.1,"publicationDate":"2023-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.com/articles/s41422-023-00871-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10145034","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}

{"title":"Development of a highly-efficient erythrocyte-drug covalent conjugation platform and its use in treating thrombotic disorders","authors":"Yanjie Huang, Xiaoqian Nie, Xuewen Liu, Yuehua Liu, Huifei Yu, Xiaofei Gao","doi":"10.1038/s41422-023-00868-2","DOIUrl":"10.1038/s41422-023-00868-2","url":null,"abstract":"","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":"33 11","pages":"887-890"},"PeriodicalIF":44.1,"publicationDate":"2023-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10153456","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}

{"title":"Structural basis of nucleosome deacetylation and DNA linker tightening by Rpd3S histone deacetylase complex","authors":"Shuqi Dong, Huadong Li, Meilin Wang, Nadia Rasheed, Binqian Zou, Xijie Gao, Jiali Guan, Weijie Li, Jiale Zhang, Chi Wang, Ningkun Zhou, Xue Shi, Mei Li, Min Zhou, Junfeng Huang, He Li, Ying Zhang, Koon Ho Wong, Xiaofei Zhang, William Chong Hang Chao, Jun He","doi":"10.1038/s41422-023-00869-1","DOIUrl":"10.1038/s41422-023-00869-1","url":null,"abstract":"In Saccharomyces cerevisiae, cryptic transcription at the coding region is prevented by the activity of Sin3 histone deacetylase (HDAC) complex Rpd3S, which is carried by the transcribing RNA polymerase II (RNAPII) to deacetylate and stabilize chromatin. Despite its fundamental importance, the mechanisms by which Rpd3S deacetylates nucleosomes and regulates chromatin dynamics remain elusive. Here, we determined several cryo-EM structures of Rpd3S in complex with nucleosome core particles (NCPs), including the H3/H4 deacetylation states, the alternative deacetylation state, the linker tightening state, and a state in which Rpd3S co-exists with the Hho1 linker histone on NCP. These structures suggest that Rpd3S utilizes a conserved Sin3 basic surface to navigate through the nucleosomal DNA, guided by its interactions with H3K36 methylation and the extra-nucleosomal DNA linkers, to target acetylated H3K9 and sample other histone tails. Furthermore, our structures illustrate that Rpd3S reconfigures the DNA linkers and acts in concert with Hho1 to engage the NCP, potentially unraveling how Rpd3S and Hho1 work in tandem for gene silencing.","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":"33 10","pages":"790-801"},"PeriodicalIF":44.1,"publicationDate":"2023-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10542350/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10145036","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}

{"title":"Heartbreakers: innate sensors ZBP1 and cGAS linked to cardiotoxicity","authors":"Wen Chen, Thirumala-Devi Kanneganti","doi":"10.1038/s41422-023-00861-9","DOIUrl":"10.1038/s41422-023-00861-9","url":null,"abstract":"","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":"33 12","pages":"902-903"},"PeriodicalIF":44.1,"publicationDate":"2023-08-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10709570/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10005003","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}

{"title":"HSPA8 acts as an amyloidase to suppress necroptosis by inhibiting and reversing functional amyloid formation","authors":"Erpeng Wu, Wenyan He, Chenlu Wu, Zhangcheng Chen, Shijie Zhou, Xialian Wu, Zhiheng Hu, Kelong Jia, Jiasong Pan, Limin Wang, Jie Qin, Dan Liu, Junxia Lu, Huayi Wang, Jixi Li, Sheng Wang, Liming Sun","doi":"10.1038/s41422-023-00859-3","DOIUrl":"10.1038/s41422-023-00859-3","url":null,"abstract":"Ultra-stable fibrous structure is a hallmark of amyloids. In contrast to canonical disease-related amyloids, emerging research indicates that a significant number of cellular amyloids, termed ‘functional amyloids’, contribute to signal transduction as temporal signaling hubs in humans. However, it is unclear how these functional amyloids are effectively disassembled to terminate signal transduction. RHIM motif-containing amyloids, the largest functional amyloid family discovered thus far, play an important role in mediating necroptosis signal transduction in mammalian cells. Here, we identify heat shock protein family A member 8 (HSPA8) as a new type of enzyme — which we name as ‘amyloidase’ — that directly disassembles RHIM-amyloids to inhibit necroptosis signaling in cells and mice. Different from its role in chaperone-mediated autophagy where it selects substrates containing a KFERQ-like motif, HSPA8 specifically recognizes RHIM-containing proteins through a hydrophobic hexapeptide motif N(X1)φ(X3). The SBD domain of HSPA8 interacts with RHIM-containing proteins, preventing proximate RHIM monomers from stacking into functional fibrils; furthermore, with the NBD domain supplying energy via ATP hydrolysis, HSPA8 breaks down pre-formed RHIM-amyloids into non-functional monomers. Notably, HSPA8’s amyloidase activity in disassembling functional RHIM-amyloids does not require its co-chaperone system. Using this amyloidase activity, HSPA8 reverses the initiator RHIM-amyloids (formed by RIP1, ZBP1, and TRIF) to prevent necroptosis initiation, and reverses RIP3-amyloid to prevent necroptosis execution, thus eliminating multi-level RHIM-amyloids to effectively prevent spontaneous necroptosis activation. The discovery that HSPA8 acts as an amyloidase dismantling functional amyloids provides a fundamental understanding of the reversibility nature of functional amyloids, a property distinguishing them from disease-related amyloids that are unbreakable in vivo.","PeriodicalId":9926,"journal":{"name":"Cell Research","volume":"33 11","pages":"851-866"},"PeriodicalIF":44.1,"publicationDate":"2023-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10624691/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9991026","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}