Pub Date : 2025-09-25DOI: 10.1016/j.ceb.2025.102584
Christoph Anton , Franziska Lautenschläger , Rhoda J. Hawkins
Here we give an overview of recent theoretical and experimental work on modeling the mechanics and dynamics of the cytoskeleton. The cytoskeleton is a multicomponent, complex and active material that is essential to cell mechanics and dynamics. We focus on one of the main components of this material, namely actin filaments. We discuss these filaments and their interactions with other proteins within the cytoskeleton. To fully understand the cytoskeleton, it is important to consider both theoretical and experimental work in calculo, in silico, in vitro, in vivo, and in situ. We review the current state of knowledge and look forward to further work to come on aspects not yet understood.
{"title":"Modeling cytoskeletal and cell dynamics","authors":"Christoph Anton , Franziska Lautenschläger , Rhoda J. Hawkins","doi":"10.1016/j.ceb.2025.102584","DOIUrl":"10.1016/j.ceb.2025.102584","url":null,"abstract":"<div><div>Here we give an overview of recent theoretical and experimental work on modeling the mechanics and dynamics of the cytoskeleton. The cytoskeleton is a multicomponent, complex and active material that is essential to cell mechanics and dynamics. We focus on one of the main components of this material, namely actin filaments. We discuss these filaments and their interactions with other proteins within the cytoskeleton. To fully understand the cytoskeleton, it is important to consider both theoretical and experimental work in calculo, in silico, in vitro, in vivo, and in situ. We review the current state of knowledge and look forward to further work to come on aspects not yet understood.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"97 ","pages":"Article 102584"},"PeriodicalIF":4.3,"publicationDate":"2025-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145159810","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 : 2025-09-22DOI: 10.1016/j.ceb.2025.102582
Syed N. Barmaver, Guoqiang Gu, Irina Kaverina
Pancreatic β cells are essential for glucose homeostasis through the regulated secretion of insulin in response to rising glucose levels. A critical component of this process is the precise and timely positioning of insulin secretory granules (ISGs) at the secretion sites on the plasma membrane. This positioning is mediated by molecular motors that transport ISGs along cytoskeletal tracks, including microtubules (MTs) and actin filaments. Despite their importance, the roles of molecular motors in insulin-secreting β cells remain incompletely understood. In this review, we summarize current findings on the involvement of molecular motors both in ISG transport, directly regulating granule availability for secretion, and in the organization of other subcellular structures, thereby indirectly influencing secretion. These indirect roles include kinesin-1-mediated microtubule sliding that configures the β cell-specific MT network, the spatial organization of calcium channels, and mitochondrial positioning, among others. We also draw parallels between β cells and neurons, proposing that insights from neuronal motor protein studies can guide future research directions in β cell biology.
{"title":"Roles of molecular motors in insulin-secreting beta cells","authors":"Syed N. Barmaver, Guoqiang Gu, Irina Kaverina","doi":"10.1016/j.ceb.2025.102582","DOIUrl":"10.1016/j.ceb.2025.102582","url":null,"abstract":"<div><div>Pancreatic β cells are essential for glucose homeostasis through the regulated secretion of insulin in response to rising glucose levels. A critical component of this process is the precise and timely positioning of insulin secretory granules (ISGs) at the secretion sites on the plasma membrane. This positioning is mediated by molecular motors that transport ISGs along cytoskeletal tracks, including microtubules (MTs) and actin filaments. Despite their importance, the roles of molecular motors in insulin-secreting β cells remain incompletely understood. In this review, we summarize current findings on the involvement of molecular motors both in ISG transport, directly regulating granule availability for secretion, and in the organization of other subcellular structures, thereby indirectly influencing secretion. These indirect roles include kinesin-1-mediated microtubule sliding that configures the β cell-specific MT network, the spatial organization of calcium channels, and mitochondrial positioning, among others. We also draw parallels between β cells and neurons, proposing that insights from neuronal motor protein studies can guide future research directions in β cell biology.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"97 ","pages":"Article 102582"},"PeriodicalIF":4.3,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145119922","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 : 2025-09-13DOI: 10.1016/j.ceb.2025.102581
Victoria Sanz-Moreno, Boon Chuan Low
{"title":"Cell signaling across scales in health and disease","authors":"Victoria Sanz-Moreno, Boon Chuan Low","doi":"10.1016/j.ceb.2025.102581","DOIUrl":"10.1016/j.ceb.2025.102581","url":null,"abstract":"","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"97 ","pages":"Article 102581"},"PeriodicalIF":4.3,"publicationDate":"2025-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145049891","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 : 2025-09-09DOI: 10.1016/S0955-0674(25)00130-9
{"title":"Outside Back Cover","authors":"","doi":"10.1016/S0955-0674(25)00130-9","DOIUrl":"10.1016/S0955-0674(25)00130-9","url":null,"abstract":"","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"96 ","pages":"Article 102592"},"PeriodicalIF":4.3,"publicationDate":"2025-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145018405","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 : 2025-08-22DOI: 10.1016/j.ceb.2025.102580
Nikita Sergejevs, Pedro Carvalho
Misfolded proteins can be toxic to cells, and their accumulation is a hallmark of diseases such as neurodegeneration. Normally, protein homeostasis is maintained by quality control processes that eliminate misfolded proteins. In the endoplasmic reticulum (ER), misfolded proteins are eliminated through endoplasmic reticulum–associated degradation (ERAD). This process is mediated by ubiquitin ligase complexes that recognize substrates in the membrane and lumen of the ER and retrotranslocate them to the cytosol to mediate their ubiquitination for subsequent degradation by the proteasome. While the recognition of luminal substrates is well understood, how ERAD complexes specifically identify and select aberrant membrane proteins remains poorly defined. Here, we review examples of intramembrane substrate recognition during ERAD and discuss the principles involved.
{"title":"Mechanisms of transmembrane domain recognition during endoplasmic reticulum quality control","authors":"Nikita Sergejevs, Pedro Carvalho","doi":"10.1016/j.ceb.2025.102580","DOIUrl":"10.1016/j.ceb.2025.102580","url":null,"abstract":"<div><div>Misfolded proteins can be toxic to cells, and their accumulation is a hallmark of diseases such as neurodegeneration. Normally, protein homeostasis is maintained by quality control processes that eliminate misfolded proteins. In the endoplasmic reticulum (ER), misfolded proteins are eliminated through endoplasmic reticulum–associated degradation (ERAD). This process is mediated by ubiquitin ligase complexes that recognize substrates in the membrane and lumen of the ER and retrotranslocate them to the cytosol to mediate their ubiquitination for subsequent degradation by the proteasome. While the recognition of luminal substrates is well understood, how ERAD complexes specifically identify and select aberrant membrane proteins remains poorly defined. Here, we review examples of intramembrane substrate recognition during ERAD and discuss the principles involved.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"96 ","pages":"Article 102580"},"PeriodicalIF":4.3,"publicationDate":"2025-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144885419","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 : 2025-08-19DOI: 10.1016/j.ceb.2025.102579
Leyi Li , Arnab Ray , Shifeng Xue
DUX4 is a transcription factor with a critical role in zygotic genome activation. It is expressed briefly in early embryogenesis and shut off for the rest of life. Inappropriate reactivation of DUX4 in adult muscle cells causes facioscapulohumeral dystrophy (FSHD), a muscular dystrophy affecting up to 1 in 8000, currently with no cure. In healthy adults, DUX4 is kept repressed through a variety of epigenetic mechanisms. Here, we explore the regulation of DUX4 in both embryogenesis and adulthood to identify similarities and differences. Comparative insights into DUX4 regulation can also be gained by studying its mouse homologue, Dux, which plays a similar role in early embryogenesis. Despite being in different genomic environments, Dux and DUX4 share similar regulatory mechanisms. We propose that the mechanisms regulating Dux and DUX4 in embryogenesis could inspire novel therapeutic angles for FSHD.
{"title":"Epigenetic regulation of DUX4: From embryogenesis to muscular degeneration","authors":"Leyi Li , Arnab Ray , Shifeng Xue","doi":"10.1016/j.ceb.2025.102579","DOIUrl":"10.1016/j.ceb.2025.102579","url":null,"abstract":"<div><div>DUX4 is a transcription factor with a critical role in zygotic genome activation. It is expressed briefly in early embryogenesis and shut off for the rest of life. Inappropriate reactivation of <em>DUX4</em> in adult muscle cells causes facioscapulohumeral dystrophy (FSHD), a muscular dystrophy affecting up to 1 in 8000, currently with no cure. In healthy adults, <em>DUX4</em> is kept repressed through a variety of epigenetic mechanisms. Here, we explore the regulation of <em>DUX4</em> in both embryogenesis and adulthood to identify similarities and differences. Comparative insights into <em>DUX4</em> regulation can also be gained by studying its mouse homologue, <em>Dux</em>, which plays a similar role in early embryogenesis. Despite being in different genomic environments, <em>Dux</em> and <em>DUX4</em> share similar regulatory mechanisms. We propose that the mechanisms regulating <em>Dux</em> and <em>DUX4</em> in embryogenesis could inspire novel therapeutic angles for FSHD.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"96 ","pages":"Article 102579"},"PeriodicalIF":4.3,"publicationDate":"2025-08-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144866542","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 : 2025-07-22DOI: 10.1016/S0955-0674(25)00115-2
{"title":"Outside Back Cover","authors":"","doi":"10.1016/S0955-0674(25)00115-2","DOIUrl":"10.1016/S0955-0674(25)00115-2","url":null,"abstract":"","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"95 ","pages":"Article 102577"},"PeriodicalIF":6.0,"publicationDate":"2025-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144679055","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 : 2025-07-19DOI: 10.1016/j.ceb.2025.102568
Sarah L. Guest , Arthur T. Molines
Cell biologists use a severely undersampled population of eukaryotes as model organisms to infer cellular processes across an immense diversity. In consequence, mechanisms are defined in only a few lineages. Here, we highlight cellular behaviors not observed in model organisms. We describe examples (multicellular and protistan) from several major supergroups (TSAR, Haptista, Archaeplastida, Amorphea, Excavates), focusing on species for which quantified dynamic measurements are available. Through these examples, we discuss how these behaviors and underlying dynamics matter for the cell biology community. We aim to increase the awareness of such organisms and familiarize readers with the diversity of behaviors present in nature. By expanding the bestiary of organisms available to researchers, we can obtain a better picture of eukaryotic cells' features and capabilities.
{"title":"Leveraging phylogenetic diversity: Cellular dynamics in non-model organisms","authors":"Sarah L. Guest , Arthur T. Molines","doi":"10.1016/j.ceb.2025.102568","DOIUrl":"10.1016/j.ceb.2025.102568","url":null,"abstract":"<div><div>Cell biologists use a severely undersampled population of eukaryotes as model organisms to infer cellular processes across an immense diversity. In consequence, mechanisms are defined in only a few lineages. Here, we highlight cellular behaviors not observed in model organisms. We describe examples (multicellular and protistan) from several major supergroups (TSAR, Haptista, Archaeplastida, Amorphea, Excavates), focusing on species for which quantified dynamic measurements are available. Through these examples, we discuss how these behaviors and underlying dynamics matter for the cell biology community. We aim to increase the awareness of such organisms and familiarize readers with the diversity of behaviors present in nature. By expanding the bestiary of organisms available to researchers, we can obtain a better picture of eukaryotic cells' features and capabilities.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"96 ","pages":"Article 102568"},"PeriodicalIF":6.0,"publicationDate":"2025-07-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144663243","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 : 2025-07-16DOI: 10.1016/j.ceb.2025.102570
Carina C. Elvira , Paul M. Jenkins
The initiation and propagation of action potentials (APs) depend on the precise localization of voltage-gated sodium (NaV) and potassium (KV) channels in neurons. In neocortical pyramidal neurons, NaV1.2 and NaV1.6 are key at the axon initial segment (AIS) and nodes of Ranvier (noR), driving AP initiation and propagation. NaV1.2 also supports AP backpropagation in the soma and dendrites. Ankyrin-G anchors these channels at the AIS and noR, while new findings reveal that ankyrin-B scaffolds NaV1.2 in dendrites. This review highlights how ankyrins stabilize NaV and KV channels across neuronal domains, ensuring proper function crucial for excitability, synaptic plasticity, and signaling. Recent findings explore how ankyrins differentially localize NaV1.2 and NaV1.6, with implications for understanding neurological disorders linked to disrupted channel localization.
{"title":"Cytoskeletal scaffolding of NaVs and KVs in neocortical pyramidal neurons: Implications for neuronal signaling and plasticity","authors":"Carina C. Elvira , Paul M. Jenkins","doi":"10.1016/j.ceb.2025.102570","DOIUrl":"10.1016/j.ceb.2025.102570","url":null,"abstract":"<div><div>The initiation and propagation of action potentials (APs) depend on the precise localization of voltage-gated sodium (Na<sub>V</sub>) and potassium (K<sub>V</sub>) channels in neurons. In neocortical pyramidal neurons, Na<sub>V</sub>1.2 and Na<sub>V</sub>1.6 are key at the axon initial segment (AIS) and nodes of Ranvier (noR), driving AP initiation and propagation. Na<sub>V</sub>1.2 also supports AP backpropagation in the soma and dendrites. Ankyrin-G anchors these channels at the AIS and noR, while new findings reveal that ankyrin-B scaffolds Na<sub>V</sub>1.2 in dendrites. This review highlights how ankyrins stabilize Na<sub>V</sub> and K<sub>V</sub> channels across neuronal domains, ensuring proper function crucial for excitability, synaptic plasticity, and signaling. Recent findings explore how ankyrins differentially localize Na<sub>V</sub>1.2 and Na<sub>V</sub>1.6, with implications for understanding neurological disorders linked to disrupted channel localization.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"96 ","pages":"Article 102570"},"PeriodicalIF":6.0,"publicationDate":"2025-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144633763","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 : 2025-07-15DOI: 10.1016/j.ceb.2025.102569
Jessica A. Cross , Derek N. Woolfson , Mark P. Dodding
Cells depend on a complex and precisely regulated subcellular organization, largely driven by the cytoskeleton and motor proteins that control intracellular transport. This review explores innovative strategies to manipulate cellular architecture using targeted protein design and engineering of cytoskeletal elements and molecular motors. We highlight advances in inducible dimerization techniques, which enable precise control over cytoskeletal dynamics through light- and small-molecule-sensitive domains. In addition, we discuss modifications to motor proteins that alter directionality, processivity, and cargo specificity, providing insights into their roles in cellular transport. Rapid advances in de novo protein design offer new tools to hijack natural cytoskeletal machinery and create synthetic elements for cellular architecture, including membraneless organelles and synthetic cytoskeletal tracks. This research promises to deepen our understanding of cellular organization, uncover regulatory mechanisms, and provide new proteins for therapeutic applications and synthetic cell development.
{"title":"Controlling cell architecture with protein design","authors":"Jessica A. Cross , Derek N. Woolfson , Mark P. Dodding","doi":"10.1016/j.ceb.2025.102569","DOIUrl":"10.1016/j.ceb.2025.102569","url":null,"abstract":"<div><div>Cells depend on a complex and precisely regulated subcellular organization, largely driven by the cytoskeleton and motor proteins that control intracellular transport. This review explores innovative strategies to manipulate cellular architecture using targeted protein design and engineering of cytoskeletal elements and molecular motors. We highlight advances in inducible dimerization techniques, which enable precise control over cytoskeletal dynamics through light- and small-molecule-sensitive domains. In addition, we discuss modifications to motor proteins that alter directionality, processivity, and cargo specificity, providing insights into their roles in cellular transport. Rapid advances in <em>de novo</em> protein design offer new tools to hijack natural cytoskeletal machinery and create synthetic elements for cellular architecture, including membraneless organelles and synthetic cytoskeletal tracks. This research promises to deepen our understanding of cellular organization, uncover regulatory mechanisms, and provide new proteins for therapeutic applications and synthetic cell development.</div></div>","PeriodicalId":50608,"journal":{"name":"Current Opinion in Cell Biology","volume":"96 ","pages":"Article 102569"},"PeriodicalIF":6.0,"publicationDate":"2025-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144631536","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}
扫码关注我们
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号