Pub Date : 2025-04-06DOI: 10.1016/j.ceb.2025.102509
Ryosuke Nishimura , Pakorn Kanchanawong
Force generation and transmission in biological systems are driven by protein-based machinery organized at the nanoscale. Thus, technological advances that allow for the measurement or manipulation of molecular-scale features are key to new mechanobiological insights. Integrins, a superfamily of adhesion receptors, function by forming supramolecular complexes that mediate mechanobiological processes such as migration and matrix remodeling. This review highlights recent findings that harness advanced techniques in microscopy, nanotechnology, and biosensors to uncover nanoscale transformations that accompany integrin responses to mechanobiological stimuli. Recent discoveries are sharpening our understanding of the diverse functions and structural organization of different integrin heterodimers and their molecular partners, highlighting their critical roles in cellular processes.
{"title":"Nanoscale mechano-adaption of integrin-based cell adhesions: New tools and techniques lead the way","authors":"Ryosuke Nishimura , Pakorn Kanchanawong","doi":"10.1016/j.ceb.2025.102509","DOIUrl":"10.1016/j.ceb.2025.102509","url":null,"abstract":"<div><div>Force generation and transmission in biological systems are driven by protein-based machinery organized at the nanoscale. Thus, technological advances that allow for the measurement or manipulation of molecular-scale features are key to new mechanobiological insights. Integrins, a superfamily of adhesion receptors, function by forming supramolecular complexes that mediate mechanobiological processes such as migration and matrix remodeling. This review highlights recent findings that harness advanced techniques in microscopy, nanotechnology, and biosensors to uncover nanoscale transformations that accompany integrin responses to mechanobiological stimuli. Recent discoveries are sharpening our understanding of the diverse functions and structural organization of different integrin heterodimers and their molecular partners, highlighting their critical roles in cellular processes.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102509"},"PeriodicalIF":6.0,"publicationDate":"2025-04-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143784028","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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 : 2025-04-04DOI: 10.1016/j.ceb.2025.102508
Akhila Rajan , Jason Karpac
Inter-organ communication networks are essential for maintaining systemic homeostasis in multicellular organisms. In Drosophila melanogaster, studies of adipokines and lipoproteins reveal evolutionarily conserved mechanisms coordinating metabolism, immunity, and behavior. This mini-review focuses on two key pathways: the adipokine Unpaired 2 (Upd2) and lipoprotein-mediated signaling. Upd2, a leptin analog, mediates fat-brain communication to regulate insulin secretion, sleep, and feeding behavior. Recent work has uncovered an LC3/Atg8-dependent secretion mechanism for Upd2, linking nutrient sensing to systemic adaptation. Lipoproteins, particularly ApoLpp and LTP, function beyond lipid transport, orchestrating neural maintenance and immune responses. During infection, macrophage-derived signals trigger lipoprotein-mediated lipid redistribution to support host defense. Additionally, muscle tissue emerges as an unexpected mediator of immune-metabolic coordination through inter-organ signaling. These findings highlight the intricate cross-talk between organs required for organismal survival and suggest therapeutic strategies for metabolic disorders.
{"title":"Inter-organ communication in Drosophila: Lipoproteins, adipokines, and immune-metabolic coordination","authors":"Akhila Rajan , Jason Karpac","doi":"10.1016/j.ceb.2025.102508","DOIUrl":"10.1016/j.ceb.2025.102508","url":null,"abstract":"<div><div>Inter-organ communication networks are essential for maintaining systemic homeostasis in multicellular organisms. In <em>Drosophila melanogaster</em>, studies of adipokines and lipoproteins reveal evolutionarily conserved mechanisms coordinating metabolism, immunity, and behavior. This mini-review focuses on two key pathways: the adipokine Unpaired 2 (Upd2) and lipoprotein-mediated signaling. Upd2, a leptin analog, mediates fat-brain communication to regulate insulin secretion, sleep, and feeding behavior. Recent work has uncovered an LC3/Atg8-dependent secretion mechanism for Upd2, linking nutrient sensing to systemic adaptation. Lipoproteins, particularly ApoLpp and LTP, function beyond lipid transport, orchestrating neural maintenance and immune responses. During infection, macrophage-derived signals trigger lipoprotein-mediated lipid redistribution to support host defense. Additionally, muscle tissue emerges as an unexpected mediator of immune-metabolic coordination through inter-organ signaling. These findings highlight the intricate cross-talk between organs required for organismal survival and suggest therapeutic strategies for metabolic disorders.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102508"},"PeriodicalIF":6.0,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143767875","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-04-04DOI: 10.1016/j.ceb.2025.102506
Julia Bourdeau, Prashali Chauhan, Jennifer L. Ross
Two important mechanisms for self-organization in cells include condensation of biomolecules, such as proteins and nucleic acids into phase-separated droplets to form membraneless organelles and organization of the cytoskeletal filaments into larger-scale systems such as the actin cortex and the microtubule-based mitotic spindle. Recent publications highlight that these two intracellular organization schemes are coordinated, with condensates controlling cytoskeletal organizations and cytoskeleton organizing the condensates. Here, we focus on recent progress from the past 2 years at the interface between condensates and cytoskeleton. We split the discussion into the physical and biological principles we can learn from these recent studies.
{"title":"Learning physics and biology from cytoskeletal and condensate interactions","authors":"Julia Bourdeau, Prashali Chauhan, Jennifer L. Ross","doi":"10.1016/j.ceb.2025.102506","DOIUrl":"10.1016/j.ceb.2025.102506","url":null,"abstract":"<div><div>Two important mechanisms for self-organization in cells include condensation of biomolecules, such as proteins and nucleic acids into phase-separated droplets to form membraneless organelles and organization of the cytoskeletal filaments into larger-scale systems such as the actin cortex and the microtubule-based mitotic spindle. Recent publications highlight that these two intracellular organization schemes are coordinated, with condensates controlling cytoskeletal organizations and cytoskeleton organizing the condensates. Here, we focus on recent progress from the past 2 years at the interface between condensates and cytoskeleton. We split the discussion into the physical and biological principles we can learn from these recent studies.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102506"},"PeriodicalIF":6.0,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143767877","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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 : 2025-04-04DOI: 10.1016/j.ceb.2025.102504
Christian Ungermann , Arne Moeller
Eukaryotic cells depend on their endolysosomal system for membrane protein and organelle turnover, plasma membrane quality control, or regulation of their nutrient uptake. All material eventually ends up in the lytic environment of the lysosome for cellular recycling. At endosomes and lysosomes, the multisubunit complexes CORVET and HOPS tether membranes by binding both their cognate Rab GTPase and specific membrane lipids. Additionally, they carry one Sec1/Munc18-like subunit at their center and thus promote SNARE assembly and, subsequently, bilayer mixing. Recent structural and functional analysis provided insights into their organization and suggested how these complexes combine tethering with fusion catalysis. This review discusses the function and structural organization of HOPS and CORVET in the context of recent studies in yeast and metazoan cells.
{"title":"Structuring of the endolysosomal system by HOPS and CORVET tethering complexes","authors":"Christian Ungermann , Arne Moeller","doi":"10.1016/j.ceb.2025.102504","DOIUrl":"10.1016/j.ceb.2025.102504","url":null,"abstract":"<div><div>Eukaryotic cells depend on their endolysosomal system for membrane protein and organelle turnover, plasma membrane quality control, or regulation of their nutrient uptake. All material eventually ends up in the lytic environment of the lysosome for cellular recycling. At endosomes and lysosomes, the multisubunit complexes CORVET and HOPS tether membranes by binding both their cognate Rab GTPase and specific membrane lipids. Additionally, they carry one Sec1/Munc18-like subunit at their center and thus promote SNARE assembly and, subsequently, bilayer mixing. Recent structural and functional analysis provided insights into their organization and suggested how these complexes combine tethering with fusion catalysis. This review discusses the function and structural organization of HOPS and CORVET in the context of recent studies in yeast and metazoan cells.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102504"},"PeriodicalIF":6.0,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143767874","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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 : 2025-04-04DOI: 10.1016/j.ceb.2025.102507
Hyojun Kim, Morgan Delarue
The cytoplasm is a dense and complex milieu in which a plethora of biochemical reactions occur. Its structure is not understood so far, albeit being central to cellular functioning. In this review, we highlight a novel perspective in which the physical properties of the cytoplasm are regulated in space and time and actively contribute to cellular function. Furthermore, we underscore recent findings that the dynamic formation of local assemblies within the cytoplasm, such as condensates and polysomes, serves as a key regulator of mesoscale cytoplasmic dynamics.
{"title":"Dynamic structure of the cytoplasm","authors":"Hyojun Kim, Morgan Delarue","doi":"10.1016/j.ceb.2025.102507","DOIUrl":"10.1016/j.ceb.2025.102507","url":null,"abstract":"<div><div>The cytoplasm is a dense and complex milieu in which a plethora of biochemical reactions occur. Its structure is not understood so far, albeit being central to cellular functioning. In this review, we highlight a novel perspective in which the physical properties of the cytoplasm are regulated in space and time and actively contribute to cellular function. Furthermore, we underscore recent findings that the dynamic formation of local assemblies within the cytoplasm, such as condensates and polysomes, serves as a key regulator of mesoscale cytoplasmic dynamics.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102507"},"PeriodicalIF":6.0,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143767876","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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 : 2025-03-28DOI: 10.1016/j.ceb.2025.102505
Bryce A. Brownfield , J. Christopher Fromme
The Golgi complex is the central sorting station of eukaryotic cells. Several unique trafficking pathways direct the transport of proteins between the Golgi and the endoplasmic reticulum, plasma membrane, and endolysosomal system. In this review we highlight several recent studies that use structural biology approaches to discover and characterize novel mechanisms cells use to control the flow of traffic through the Golgi. These studies provide important new insights into how activation of Arf and Rab GTPases is regulated, how cargo proteins are sorted during vesicle biogenesis, and how vesicle tethers identify their target compartments.
{"title":"Structural insights into traffic through the Golgi complex","authors":"Bryce A. Brownfield , J. Christopher Fromme","doi":"10.1016/j.ceb.2025.102505","DOIUrl":"10.1016/j.ceb.2025.102505","url":null,"abstract":"<div><div>The Golgi complex is the central sorting station of eukaryotic cells. Several unique trafficking pathways direct the transport of proteins between the Golgi and the endoplasmic reticulum, plasma membrane, and endolysosomal system. In this review we highlight several recent studies that use structural biology approaches to discover and characterize novel mechanisms cells use to control the flow of traffic through the Golgi. These studies provide important new insights into how activation of Arf and Rab GTPases is regulated, how cargo proteins are sorted during vesicle biogenesis, and how vesicle tethers identify their target compartments.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102505"},"PeriodicalIF":6.0,"publicationDate":"2025-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143716174","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-03-20DOI: 10.1016/j.ceb.2025.102493
Catharina Küng , Michael Lazarou , Thanh Ngoc Nguyen
Mitophagy is an important lysosomal degradative pathway that removes damaged or unwanted mitochondria to maintain cellular and organismal homeostasis. The mechanisms behind how mitophagy is initiated to form autophagosomes around mitochondria have gained a lot of interest since they can be potentially targeted by mitophagy-inducing therapeutics. Mitophagy initiation can be driven by various autophagy receptors or adaptors that respond to different cellular and mitochondrial stimuli, ranging from mitochondrial damage to metabolic rewiring. This review will cover recent advances in our understanding of how mitophagy is initiated, and by doing so reveal the mechanistic plasticity of how autophagosome formation can begin.
{"title":"Advances in mitophagy initiation mechanisms","authors":"Catharina Küng , Michael Lazarou , Thanh Ngoc Nguyen","doi":"10.1016/j.ceb.2025.102493","DOIUrl":"10.1016/j.ceb.2025.102493","url":null,"abstract":"<div><div>Mitophagy is an important lysosomal degradative pathway that removes damaged or unwanted mitochondria to maintain cellular and organismal homeostasis. The mechanisms behind how mitophagy is initiated to form autophagosomes around mitochondria have gained a lot of interest since they can be potentially targeted by mitophagy-inducing therapeutics. Mitophagy initiation can be driven by various autophagy receptors or adaptors that respond to different cellular and mitochondrial stimuli, ranging from mitochondrial damage to metabolic rewiring. This review will cover recent advances in our understanding of how mitophagy is initiated, and by doing so reveal the mechanistic plasticity of how autophagosome formation can begin.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102493"},"PeriodicalIF":6.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143674886","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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 : 2025-03-20DOI: 10.1016/j.ceb.2025.102501
Xiao Wang , Tiantian Li , Yusong Guo , Xiao-Wei Chen
The secretory pathway, which begins at the endoplasmic reticulum (ER) through the COPII complex, is responsible for transporting proteins and lipid carriers to various destined cellular compartments or extracellular space. The fundamental mechanism by which the COPII operates is evolutionarily conserved. Nevertheless, the vast diversity of mammalian cargos poses significant challenges to the secretory pathway, especially considering the intricate physiology in vivo. Particularly, certain physiologically essential cargos, including procollagen and lipoproteins, appear to be oversized for these canonical carriers, implying the need for additional sophisticated regulation at the onset step so-called ER exit. Emerging evidence highlights the critical role of cargo receptors in selective sorting for ER export, illuminating the complex biology of the trafficking dynamics, which holds broad implications for human health and diseases.
{"title":"License to drive: Receptor-mediated ER exit of proteins and lipids","authors":"Xiao Wang , Tiantian Li , Yusong Guo , Xiao-Wei Chen","doi":"10.1016/j.ceb.2025.102501","DOIUrl":"10.1016/j.ceb.2025.102501","url":null,"abstract":"<div><div>The secretory pathway, which begins at the endoplasmic reticulum (ER) through the COPII complex, is responsible for transporting proteins and lipid carriers to various destined cellular compartments or extracellular space. The fundamental mechanism by which the COPII operates is evolutionarily conserved. Nevertheless, the vast diversity of mammalian cargos poses significant challenges to the secretory pathway, especially considering the intricate physiology <em>in vivo</em>. Particularly, certain physiologically essential cargos, including procollagen and lipoproteins, appear to be oversized for these canonical carriers, implying the need for additional sophisticated regulation at the onset step so-called ER exit. Emerging evidence highlights the critical role of cargo receptors in selective sorting for ER export, illuminating the complex biology of the trafficking dynamics, which holds broad implications for human health and diseases.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102501"},"PeriodicalIF":6.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143674912","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-03-10DOI: 10.1016/j.ceb.2025.102492
Julia R. Flood, Caitlin A. Mendina, Anjon Audhya
The early secretory pathway governs the transport of thousands of secreted and transmembrane proteins and lipids from the endoplasmic reticulum (ER) to juxtaposed ER-Golgi Intermediate Compartments (ERGIC). This process is largely directed by Coat Protein complex II (COPII), which accumulates on distinct, ribosome-free ER subdomains (transitional ER) to generate highly curved transport intermediates of various sizes and shapes. The rate of secretory flux from the ER can vary significantly, depending on cell type, environmental cues, and other factors, but the mechanisms that regulate COPII-mediated trafficking have been slow to emerge. Here, we focus on recent progress that has contributed to our understanding of how the early secretory pathway is structured to facilitate the export of cargoes from the ER into a chasm approximately 300–500-nm in size, prior to fusion with ERGIC membranes without the aid of cytoskeletal elements to guide their journey.
早期分泌途径控制着数千种分泌蛋白、跨膜蛋白和脂质从内质网（ER）向并列的ER-高尔基中间区室（ERGIC）的运输。这一过程主要由衣壳蛋白复合物 II（COPII）引导，COPII 在不同的、无核糖体的 ER 亚域（过渡 ER）上聚集，生成各种尺寸和形状的高度弯曲的运输中间体。ER分泌通量的速率会因细胞类型、环境线索和其他因素的不同而发生显著变化，但调控COPII介导的转运的机制却迟迟没有出现。在此，我们将重点介绍最近的研究进展，这些进展有助于我们了解早期分泌途径的结构是如何促进货物从ER输出到约300-500纳米大小的鸿沟中，然后与ERGIC膜融合，而无需借助细胞骨架元件来引导货物的旅程。
{"title":"Organizing principles underlying COPII-mediated transport","authors":"Julia R. Flood, Caitlin A. Mendina, Anjon Audhya","doi":"10.1016/j.ceb.2025.102492","DOIUrl":"10.1016/j.ceb.2025.102492","url":null,"abstract":"<div><div>The early secretory pathway governs the transport of thousands of secreted and transmembrane proteins and lipids from the endoplasmic reticulum (ER) to juxtaposed ER-Golgi Intermediate Compartments (ERGIC). This process is largely directed by Coat Protein complex II (COPII), which accumulates on distinct, ribosome-free ER subdomains (transitional ER) to generate highly curved transport intermediates of various sizes and shapes. The rate of secretory flux from the ER can vary significantly, depending on cell type, environmental cues, and other factors, but the mechanisms that regulate COPII-mediated trafficking have been slow to emerge. Here, we focus on recent progress that has contributed to our understanding of how the early secretory pathway is structured to facilitate the export of cargoes from the ER into a chasm approximately 300–500-nm in size, prior to fusion with ERGIC membranes without the aid of cytoskeletal elements to guide their journey.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102492"},"PeriodicalIF":6.0,"publicationDate":"2025-03-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143576800","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-03-09DOI: 10.1016/j.ceb.2025.102488
Aurélie Dobric, Christopher J. Tape
Cellular phenotypes are regulated by dynamic signalling processes that involve proteins, post-translational modifications, epigenetic events, and transcriptional responses. Functional perturbation studies are required to understand cell signalling mechanisms and organoids have recently emerged as scalable biomimetic models amenable to large-scale perturbation. Here, we review the recent advances in high-dimensional analysis of cell signalling in organoids. Single-cell technologies provide cell-type specific analysis of multiple biochemical modalities, enabling a deeper understanding of the signalling mechanisms driving cell-fate dynamics. Emerging multimodal techniques are further revealing coordination between signalling layers and are poised to increase our mechanistic understanding of cell signalling.
{"title":"High-dimensional signalling analysis of organoids","authors":"Aurélie Dobric, Christopher J. Tape","doi":"10.1016/j.ceb.2025.102488","DOIUrl":"10.1016/j.ceb.2025.102488","url":null,"abstract":"<div><div>Cellular phenotypes are regulated by dynamic signalling processes that involve proteins, post-translational modifications, epigenetic events, and transcriptional responses. Functional perturbation studies are required to understand cell signalling mechanisms and organoids have recently emerged as scalable biomimetic models amenable to large-scale perturbation. Here, we review the recent advances in high-dimensional analysis of cell signalling in organoids. Single-cell technologies provide cell-type specific analysis of multiple biochemical modalities, enabling a deeper understanding of the signalling mechanisms driving cell-fate dynamics. Emerging multimodal techniques are further revealing coordination between signalling layers and are poised to increase our mechanistic understanding of cell signalling.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"94 ","pages":"Article 102488"},"PeriodicalIF":6.0,"publicationDate":"2025-03-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143576799","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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