Cell Death and Differentiation最新文献

{"title":"The NEK8/ALYREF axis promotes cisplatin resistance in bladder cancer by stabilizing CDK18 mRNA to facilitate DNA damage repair.","authors":"Jia-Yin Chen, Zhi-Bin Ke, Bin Lin, Meng-Xin Liu, Zi-Heng Yan, Yu-Xuan Zhao, Chao-Ran Chen, Xue-Yi Xue, Qing-Shui Zheng, Yong Wei, Hai Cai, Ning Xu","doi":"10.1038/s41418-026-01883-7","DOIUrl":"https://doi.org/10.1038/s41418-026-01883-7","url":null,"abstract":"<p><p>Cisplatin-based chemotherapy remains a standard treatment for advanced bladder cancer (BCa), however, the development of chemoresistance substantially compromises its clinical efficacy and patient prognosis. In this study, we investigated the functional role of NEK8 in cisplatin resistance in BCa and elucidated its underlying molecular mechanisms. We found that NEK8 was significantly upregulated in cisplatin-resistant BCa and was associated with unfavorable prognosis. Functional studies demonstrated that NEK8 promoted cisplatin resistance and tumor progression both in vitro and in vivo. Mechanistically, NEK8 directly interacted with ALYREF and promoted its phosphorylation and subsequent nuclear translocation. Nuclear ALYREF recognized m5C-modified CDK18 mRNA and enhanced its stability, resulting in increased CDK18 expression. Elevated CDK18 facilitated DNA damage repair, ultimately driving cisplatin resistance in BCa. Collectively, we identified a NEK8-mediated mechanism in which ALYREF phosphorylation and nuclear translocation enhance CDK18 mRNA stability and DNA damage repair, thereby driving cisplatin resistance in BCa.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":13.6,"publicationDate":"2026-10-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149223433","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":"PABPC1 dictates castration sensitivity in prostate cancer via orchestrating ferroptosis resistance and CD8(+) T-cell dysfunction.","authors":"Tianlong Luo, Qianghua Zhou, Bisheng Cheng, Jianhan Fu, Yong Luo, Jintao Hu, Haitao Zhong, Yongxin Wu, Xuesen Dong, Zhiming Wu, Hao Huang, Kai Yao, Haixia He, Hai Huang","doi":"10.1038/s41418-026-01870-y","DOIUrl":"https://doi.org/10.1038/s41418-026-01870-y","url":null,"abstract":"<p><p>Resistance to next-generation androgen receptor antagonists represents a major clinical challenge in prostate cancer (PCa), underscoring the need to define its underlying mechanisms. Here, through an integrated analysis of multiple cohorts, we identify PABPC1 as an RNA-binding protein upregulated in therapy-resistant tumors, whose expression correlates with adverse clinicopathological features. Elevated PABPC1 confers enzalutamide (Enz) resistance by suppressing tumor-cell ferroptosis and CD8⁺ T-cell cytotoxicity. Mechanistically, PABPC1 promotes the cytoplasmic colocalization of EIF4A1 with ATF4 mRNA and enhances EIF4A1-associated translation of ATF4 mRNA. Subsequently, ATF4 binds the BCAT1 promoter and transcriptionally upregulates BCAT1, thereby promoting branched-chain amino acid (BCAA) metabolic remodeling and ferroptosis resistance, with leucine emerging as a major functional contributor to both ferroptosis regulation and CD8⁺ T-cell effector responses. In preclinical models, ixazomib restores ferroptotic vulnerability, reinvigorates T-cell activity, and synergizes with Enz, without overt histopathological abnormalities in major organs. These results identify the PABPC1-ATF4-BCAT1 axis as a key regulatory pathway linking RNA regulation with metabolic and immune reprogramming to facilitate treatment resistance in PCa.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":13.6,"publicationDate":"2026-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149206621","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":"A chemical-genetic system for calreticulin exposure on cancer cells reveals immune-dependent antitumor effects.","authors":"Liwei Zhao, Misha Mao, Zhe Shen, Yuhong Pan, Ke Chai, Oliver Kepp, Guido Kroemer, Peng Liu","doi":"10.1038/s41418-026-01891-7","DOIUrl":"https://doi.org/10.1038/s41418-026-01891-7","url":null,"abstract":"<p><p>Premortem exposure of calreticulin (CALR) on stressed cancer cells is a cardinal damage-associated molecular pattern that licenses anticancer immunity, yet its immunological sufficiency has remained difficult to define because it normally coincides with cellular stress and cell death. Here, we engineered a chemical-genetic system enabling the conditional, biotin-driven translocation of a membrane-anchored CALR chimera from the endoplasmic reticulum to the plasma membrane, thereby uncoupling CALR exposure from cytotoxicity and other hallmarks of immunogenic cell death. This reductionist approach revealed that isolated CALR surface presentation is sufficient to promote CD91/LRP1-dependent engulfment of tumor cells by conventional dendritic cells, particularly cDC1 and cDC2, leading to enhanced dendritic cell activation, cytotoxic lymphocyte responses, and immunological memory. Across multiple syngeneic tumor models, enforced CALR exposure exerted modest standalone antitumor activity but robustly sensitized poorly immunogenic cancers to cisplatin and PD-1 blockade, culminating in T cell-dependent tumor eradication and durable protective immunity. Remarkably, concurrent inhibition of the CD47-SIRPα axis facilitated complete tumor eradication in all treated animals, highlighting the functional cooperation between eat-me and don't-eat-me signals in orchestrating antigen presentation and adaptive immune priming. These findings further suggest that maximizing the therapeutic activity of CD47 blockade may require concomitant reinforcement of pro-phagocytic signals such as CALR exposure, providing a conceptual framework for the rational design of next-generation combination immunotherapies. Collectively, these findings establish surface-exposed CALR as a cell-autonomous immunogenic signal with instructive activity for dendritic cell-mediated cross-priming and provide a tractable platform to mechanistically deconvolute immunogenic stress responses, with immediate implications for the rational design of combinatorial chemo- and immunotherapeutic regimens in preclinical and potentially clinical oncology.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":13.6,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149191510","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":"USP25 augments XIAP-mediated signaling to safeguard intestinal homeostasis.","authors":"Jiangyun Shen, Deyu Deng, Deqi Wang, Jianzhao Zhang, Yimin Lin, Liyan Lou, Yanqi Xu, Lili Ma, Zijun Cao, Keshuo Jin, Fuqi Mei, Jiaqing Chen, Jun Xu, Wenhua Zheng, Jing Ruan, Yangping Shentu, Xu Wang","doi":"10.1038/s41418-026-01885-5","DOIUrl":"https://doi.org/10.1038/s41418-026-01885-5","url":null,"abstract":"<p><p>Nucleotide-binding oligomerization domain containing 2 (NOD2) recognizes conserved bacterial components in the cytoplasm to initiate innate immune responses, and its mutations are closely associated with Crohn's disease (CD). Here, we discover that the NOD2 signaling is regulated by the deubiquitinase USP25. Macrophages lacking USP25 exhibit impaired NOD2 signaling and are defective in cytokine production upon stimulation with muramyl dipeptide (MDP). USP25 enhances NOD2-initiated signal transduction by increasing the expression and recruitment of X-linked inhibitor of apoptosis protein (XIAP). In mice, USP25 deficiency exacerbates intestinal inflammation induced by 2,4,6-trinitrobenzenesulfonic acid (TNBS), whereas USP25 overexpression alleviates TNBS-induced colitis. Moreover, USP25 deficiency leads to spontaneous intestinal inflammation in aged mice. Importantly, a known single nucleotide polymorphism associated with human inflammatory bowel disease compromises USP25 expression, and lower USP25 expression is detected in patients with CD. Thus, USP25 plays a critical role in NOD2 signaling and may represent a potential therapeutic target for CD.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":13.6,"publicationDate":"2026-10-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149179649","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":"Death domain-mediated higher-order oligomerization of RIPK1 drives TNF-induced signaling.","authors":"Ying Chen, Jianwei Li, Yaw Bia Tan, Lihua Lai, Ping Liu, Ita Novita Sari, Anandhkumar Raju, Vinh Thang Huynh, Amhed Missael Vargas Velazquez, Samuel Jianjie Yeo, Dahai Luo, Vinay Tergaonkar","doi":"10.1038/s41418-026-01889-1","DOIUrl":"https://doi.org/10.1038/s41418-026-01889-1","url":null,"abstract":"<p><p>RIPK1 paradoxically orchestrates pro-survival and pro-death pathways through its scaffolding and kinase activities. Downstream of TNFR1, RIPK1 initiates the formation of two distinct multiprotein complexes: complex I for cell survival and complex IIa/IIb for apoptosis or necroptosis. However, the molecular architecture that initiates RIPK1-mediated assembly of these multiprotein signaling complexes remains unknown. Here, we elucidate the filamentous structure of the death domain of RIPK1 (^RIPK1DD) at 2.5 Å resolution using cryogenic electron microscopy (cryo-EM). ^RIPK1DD filaments comprise three helical chains assembled via four distinct types of interactions, including a unique, hitherto undescribed Type IV interaction. Structure-guided mutagenesis of interface residues effectively disrupts ^RIPK1DD filament formation, impairs RIPK1 recruitment and ubiquitination within TNFR1 complex I, and abrogates TNF-induced transcriptional responses. Furthermore, death domain-mediated higher-order oligomerization drives RIPK1 autophosphorylation, which consequently licenses the assembly of complex IIa and complex IIb to execute apoptosis and necroptosis, respectively. Together, these findings reveal a critical structural basis of death domain-mediated RIPK1 oligomerization and provide fundamental mechanistic insights into RIPK1-mediated assembly of signaling complexes downstream of TNFR1.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":13.6,"publicationDate":"2026-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149135188","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":"nHOTAIRM1 scaffolds ANXA11-dependent assemblies to drive axonal mRNA localization in human motor neurons","authors":"Paolo Tollis, Tiziana Santini, Adriano Setti, Walter Visciglio, Jessica Rea, Davide Mariani, Alessandro Belvedere, Monica Ballarino, Irene Bozzoni, Pietro Laneve","doi":"10.1038/s41418-026-01880-w","DOIUrl":"https://doi.org/10.1038/s41418-026-01880-w","url":null,"abstract":"Long noncoding RNAs (lncRNAs) are well recognized as regulators of neuronal development and function, yet their integration into canonical axonal transport pathways, an essential component of spatial gene regulation in highly polarized cells, remains incompletely defined. It is still unclear to what extent individual lncRNAs confer cargo selectivity and couple discrete mRNA cohorts to established transport machineries. Here we identify a cytoplasmic role for the neuronal isoform of the lncRNA HOTAIRM1 (nHOTAIRM1) in shaping the axonal RNA landscape of human induced pluripotent stem cell -derived spinal motor neurons (spMNs). We show that nHOTAIRM1 associates with Annexin A11 (ANXA11), a factor linked to lysosome-coupled movement of RNA granules, and engages a defined subset of motor neuron-relevant mRNAs. Transcriptome-wide and targeted interaction assays, together with computational mapping and steric competition, support direct RNA-RNA pairing between nHOTAIRM1 and mRNAs involved in cytoskeletal organization and synaptic or vesicular functions, while spatial analyses place these RNA pairs in close proximity within the soma and neurites. Loss-of-function experiments further show that nHOTAIRM1 depletion reduces the association of these mRNAs with ANXA11-positive complexes and diminishes their enrichment in neuronal projections, an effect that is recapitulated by ANXA11 depletion. Collectively, these findings support a model in which nHOTAIRM1 contributes to the selective recruitment of cargo mRNAs into ANXA11-associated transport assemblies, thereby promoting their localization within distal neurites. More broadly, our findings provide mechanistic insight into how a lncRNA can regulate mRNA sorting, and compartment-specific RNA trafficking in human spMNs.","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"1 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149087630","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":"Ubiquitination of LMP-1 by UFD-2 regulates apoptotic cell clearance","authors":"Lei Yuan, Peiyao Li, Xinyan Li, Yingying Xi, Fuqiao Liu, Qian Zheng, Hui Wang, Hui Xiao","doi":"10.1038/s41418-026-01886-4","DOIUrl":"https://doi.org/10.1038/s41418-026-01886-4","url":null,"abstract":"Apoptotic cell clearance, or efferocytosis, is essential for tissue homeostasis and preventing inflammation in multicellular organisms. Through a genome-wide RNAi screen targeting 169 E3 ubiquitin ligases in Caenorhabditis elegans, we identified six ligases involved in efferocytosis regulation, with UFD-2 deletion showing the most significant defect. UFD-2 was found to be critical for phagosome maturation and degradation during apoptotic cell clearance. We identified the lysosomal membrane protein LMP-1 as a direct substrate of UFD-2 and showed that UFD-2 cooperates with UBC-15 to catalyze K63-linked polyubiquitination of LMP-1, essential for efficient apoptotic cell clearance. Loss of UFD-2 resulted in reduced LMP-1 levels within lysosomes and impaired activation of lysosomal DNase NUC-1. The function of UFD-2 in efferocytosis is evolutionarily conserved, as its mammalian homolog UBE4B similarly regulates apoptotic cell clearance in macrophages. These findings establish UFD-2 as a key regulator of efferocytosis, providing therapeutic insights into diseases associated with defective efferocytosis.","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"1 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149087634","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":"Synergistic role of TFEB/TFE3 and mTORC1 in kidney cystogenesis and tumorigenesis","authors":"Marco Ferniani, Irene Sambri, Tuong Huynh, Rossella Pennella, Gennaro Tufano, Niculin J. Herz, Barbara Rossi, Antonella Iannaccone, Francesco Trepiccione, Alessia Calcagnì, Andrea Ballabio","doi":"10.1038/s41418-026-01881-9","DOIUrl":"https://doi.org/10.1038/s41418-026-01881-9","url":null,"abstract":"Birt-Hogg-Dubé (BHD) and Tuberous Sclerosis (TSC) are inherited cancer syndromes associated with kidney cystogenesis and tumorigenesis and caused by mutations of the folliculin (FLCN) and TSC1/2 genes, respectively. We and others previously showed that Transcription Factors EB (TFEB) and E3 (TFE3) are the main drivers of the kidney phenotypes observed in mouse models of these conditions. These transcription factors are also responsible for the feedback hyperactivation of the mechanistic Target of Rapamycin Complex 1 (mTORC1), a known tumorigenic factor. This raises the question of whether TFEB/TFE3 exert their oncogenic activity by inducing mTORC1 or by mTORC1-independent pathways. To address this question, we generated kidney-specific mouse models in which we knocked out factors that differentially control mTORC1 and TFEB/TFE3, thus uncoupling their activities. Specifically, we generated three kidney-specific conditional knockout lines: (1) Depdc5-KO mice in which loss of GATOR1 activity leads to mTORC1 hyperactivation and TFEB/TFE3 inhibition, (2) RagC-KO mice in which TFEB/TFE3 are constitutively active and mTORC1 activity is partially inhibited due to impaired Rag heterodimer formation, and (3) Flcn/RagC double KO mice to test whether mTORC1 inhibition induced by RagC loss ameliorates the aggressive kidney phenotype of FLCN KO mice. Comparison between these models revealed that mTORC1 hyperactivation is a key driver of cystogenesis and tumorigenesis, while TFEB/TFE3 constitutive activation further enhances and accelerates pathology by establishing a transcriptional program that integrates metabolic and stress-response pathways. Together, our findings define an oncogenic mechanism by which both mTORC1 and TFEB/TFE3 hyperactivation cooperate in kidney tumorigenesis.","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"8 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2026-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149087628","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":"FDX1-short proteoform induces caspase-independent cell death in tumor cells","authors":"Jing-xia Han, Yu Sun, Zhen Yang, Ya-xin Sun, Zi-cheng Zhao, Zi-ting Hao, Ting Wu, Wei-long Zhong, Xiao-hui Hou, An-yang Wang, Hui-juan Liu, Da-qing Sun, Ming Gao, Tao Sun, Heng Zhang","doi":"10.1038/s41418-026-01856-w","DOIUrl":"https://doi.org/10.1038/s41418-026-01856-w","url":null,"abstract":"Cell death is a crucial process for the maintenance of physiological functions in organisms. In recent years, cuproptosis, a novel form of cell death induced by copper overload in mitochondria, has emerged as a critical regulatory mechanism. Ferredoxin 1 (FDX1), a key electron transfer protein in this pathway, is essential for copper metabolism and the regulation of cuproptosis. In this study, we characterized a natural short proteoform of FDX1, FDX1-Short Proteoform (FDX1-SP). Lacking the canonical N-terminal mitochondrial targeting sequence, FDX1-SP is widely distributed throughout the cell, with a pronounced propensity for nuclear accumulation. The accumulation of FDX1-SP protein triggers cleavage and degradation of tumor cell DNA. This disrupts nuclear membrane integrity and induces cell death in a caspase-independent manner. FDX1-SP preferentially damages highly accessible chromatin regions in tumor cells, thereby inducing tumor cell death. Based on these findings, we developed an FDX1-SP mRNA therapeutic, which exhibited significant DNA damage and anti-tumor effects in patient-derived xenograft (PDX) models. Our research uncovers the mechanism of death mediated by FDX1-SP, providing new directions for tumor therapy.","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"11 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2026-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149087629","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":"Efferocytosis triggered proteomic reprogramming of macrophages reveals CD97 as a novel apoptotic receptor.","authors":"Benjamin Bernard Armando Raymond, Jasmin Novenstern, Abeer Dannoura, Meihan Meng, Andrew Michael Frey, Tamara Sneperger, Luigi Zechini, Alessandro Scopelliti, Will Wood, Matthias Trost","doi":"10.1038/s41418-026-01882-8","DOIUrl":"https://doi.org/10.1038/s41418-026-01882-8","url":null,"abstract":"<p><p>During the daily process of healthy cellular turnover in the human body, billions of cells undergo apoptosis. These cells are removed by phagocytic cells, namely macrophages through a process known as efferocytosis, which triggers a cascade of reprogramming events in the cell, with a shift towards a pro-resolving or 'wound healing' phenotype. To date, no study has attempted to investigate these phenotypic changes from a proteomic perspective. Here, we present a novel and robust workflow for the investigation of proteome and secretome changes in bone marrow-derived macrophages (BMDMs) and alveolar macrophages following efferocytosis using stable isotope labelling by amino acids in cell culture (SILAC) combined with data-independent acquisition (DIA) mass spectrometry. Using this workflow, we dissected the mixed proteomes of BMDMs and apoptotic cells to map the reprogramming events occurring in macrophages in the later stages of efferocytosis. Specifically, we identified the adhesion G protein-coupled receptor Adgre5/CD97 as a novel efferocytosis-associated protein and showed that this evolutionary conserved protein plays a role in the uptake of apoptotic cells (ACs) by macrophages from mouse, human and fly. Additionally, we show that CD97 may act as a co-receptor for ACs with other efferocytic receptors such as MerTK. Our results provide an unprecedented view of the efferocytic landscape of macrophages and will aid in further understanding this important immunological process in the larger context of immune homeostasis and inflammatory disorders.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":13.6,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149079789","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}