Cytoskeleton (Hoboken, N.J.)最新文献_第7页

Engineering and Characterization of a Fluorescent Fission Yeast Arp2/3 Complex for Single Molecule Mechanistic Investigations. 用于单分子机制研究的荧光裂变酵母Arp2/3复合物的工程和表征。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-03-08 DOI: 10.1002/cm.70120

Caitlin A Anderson, Meghan E O'Connell, Kaitlin E Homa, Cristian Suarez, Michael L James, Kashmeera D Baboolall, Vilmos Zsolnay, Vladimir Sirotkin, David R Kovar

{"title":"Engineering and Characterization of a Fluorescent Fission Yeast Arp2/3 Complex for Single Molecule Mechanistic Investigations.","authors":"Caitlin A Anderson, Meghan E O'Connell, Kaitlin E Homa, Cristian Suarez, Michael L James, Kashmeera D Baboolall, Vilmos Zsolnay, Vladimir Sirotkin, David R Kovar","doi":"10.1002/cm.70120","DOIUrl":"10.1002/cm.70120","url":null,"abstract":"Arp2/3 complex is a seven-component protein complex that facilitates the assembly of branched actin filament networks by binding to pre-existing \"mother\" actin filaments and initiating the nucleation of new branched \"daughter\" filaments. Arp2/3 complex must be activated by a nucleation promoting factor such as the WASP/Scar protein family. The direct visualization of Arp2/3 complex during the branching pathway is critical to elucidate the underlying molecular mechanisms under diverse assembly conditions. Here we have successfully purified and fluorescently labeled a fission yeast Arp2/3 complex that is activated by different classes of fission yeast nucleation promoting factors. We visualized Arp2/3 complex actin filament binding and branch formation in two-color TIRF microscopy assays, revealing that a single complex of Arp2/3 complex nucleates a branched actin filament ~2 s after binding. We have therefore generated an important reagent that can help elucidate a clearer understanding of the pathway and regulation of Arp2/3 complex-mediated actin filament branch formation.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":1.6,"publicationDate":"2026-03-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147379482","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

CiliaNet CZ-Cilia and Flagella Research Network in the Czech Republic. 捷克共和国的纤毛和鞭毛研究网络。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-03-06 DOI: 10.1002/cm.70121

Tomáš Bárta, Michaela Bosáková, Marcela Buchtová, Lukáš Čajánek, Aniruddha Mitra, Jiří Uhlík, Vladimír Varga, Martina Huranová

引用次数: 0

Domain-Level Interaction of FAP174 (MYCBP-1) and FAP147 (MYCBPAP) Proteins of the C2a Projection of Chlamydomonas Cilia. 纤毛衣单胞菌C2a投射蛋白FAP174 （MYCBP-1）和FAP147 （MYCBPAP）结构域水平的相互作用

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-02-22 DOI: 10.1002/cm.70112

Sneha Desai, Abhay Pal, Hridhya Nair, Sarath Chandra Dantu, Jacinta S D'Souza

{"title":"Domain-Level Interaction of FAP174 (MYCBP-1) and FAP147 (MYCBPAP) Proteins of the C2a Projection of Chlamydomonas Cilia.","authors":"Sneha Desai, Abhay Pal, Hridhya Nair, Sarath Chandra Dantu, Jacinta S D'Souza","doi":"10.1002/cm.70112","DOIUrl":"https://doi.org/10.1002/cm.70112","url":null,"abstract":"The C2a projection of the central pair of flagella in Chlamydomonas reinhardtii harbours the A-kinase anchoring protein FAP65, FAP174, FAP147 and FAP70. FAP174, an RII-like protein with its N-terminal dimerization and docking domain, binds to the amphipathic helices of FAP65. Cryo-EM data do not reveal the entire sequences for FAP174 and FAP147. Hence, the interacting domains within this scaffold remain elusive. This study has identified the interacting domains of FAP174 with FAP147. The FAP147 protein and its MYCBPAP domain (129-639 a.a.) bind to the C-terminus of FAP174 (47-92 a.a.). In silico docking analyses using CABS-Dock to delineate the interaction identified several MYCBPAP-derived peptides, such as p3 (310-339), p4 (319-348), p9 (547-576), p13 (528-557) and p15 (350-379), to form stable interacting complexes with RMSD < 3 Å 2-3 times, and are potentially amphipathic. To gain atomistic details of the interaction, molecular dynamics (MD) simulations of the FAP147 MYCBPAP domain in complex with the FAP174 C-terminus were performed. It revealed stable interfacial contacts, a subset of which overlap with residues within the p15 peptide region of the MYCBPAP domain, while identifying G48, S49, P52, Y55, L79, Q80 and V83 as key interacting residues within the C-terminus of FAP174. Individual alanine substitution of the FAP174 residues, followed by overlay assay with FAP147, retained the interaction, indicating that the interaction does not depend solely on discrete amino acids but on broader interface interactions.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":1.6,"publicationDate":"2026-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147273171","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Filamin C Modulates Cellular Mechanoresponse Through Focal Adhesion Turnover and Actin Stabilization. 丝蛋白C通过黏附转换和肌动蛋白稳定调节细胞机械反应。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-02-22 DOI: 10.1002/cm.70110

E S Klimenko, M Yu Sorokina, K S Sukhareva, N A Smolina, I A Makhnin, T Sejersen, A A Kostareva

{"title":"Filamin C Modulates Cellular Mechanoresponse Through Focal Adhesion Turnover and Actin Stabilization.","authors":"E S Klimenko, M Yu Sorokina, K S Sukhareva, N A Smolina, I A Makhnin, T Sejersen, A A Kostareva","doi":"10.1002/cm.70110","DOIUrl":"https://doi.org/10.1002/cm.70110","url":null,"abstract":"The study aimed to elucidate the mechanistic basis of impaired mechanosensitive pathways-YAP/TAZ and β-catenin signaling-in filamin C-deficient cells through investigation of transcriptomic profiles, actin cytoskeleton organization and focal adhesion structure. By using FlncKO-C2C12 cells and testing a number of inhibitors, we identified that mechanosensitive processes depend on filamin C function. We detected that filamin C deficiency leads to increased F/G-actin ratio and expansion of focal adhesion structures along with diminished nuclear accumulation of TAZ and β-catenin and decreased YAP/TAZ activity. Verteporfin-mediated YAP/TAZ inhibition caused adhesion enlargement and slight elevation of F/G-actin ratio in WT-C2C12 but had lower efficiency in FlncKO-C2C12. Of note, actin cytoskeletal stabilization through Jasplakinolide treatment rescued YAP/TAZ signaling specifically in filamin C-deficient cells, whereas inhibition of non-muscle myosin II with (-)Blebbistatin failed to recapitulate the signaling suppression observed in control cells. In addition, ROCK inhibition with Y-27632 demonstrated greater focal adhesion disassembly in FlncKO-C2C12 cells than in WT-C2C12 and produced a genotype-specific response, restoring β-catenin nuclear localization exclusively in FlncKO-C2C12 without affecting WT-C2C12 cells. In summary, we propose that in C2C12 muscle cells filamin C deficiency causes aberrant focal adhesion turnover and impairs actomyosin complex stabilization, which together compromise mechanosensitive pathways-YAP/TAZ and β-catenin-and affect differentiation potential of muscle cells already at the myoblast stage.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":1.6,"publicationDate":"2026-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147273200","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Cytoskeleton Spotlight: Edward Buckley. 细胞骨架：Edward Buckley。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-02-19 DOI: 10.1002/cm.70108

Edward Buckley

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Evolving With Septins: Interview With Michelle Momany. 与septin一起进化：采访Michelle Momany。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-02-19 DOI: 10.1002/cm.70101

Michelle Momany, Michaela Horger, Ondřej Kučera

引用次数: 0

GIP Affects Neuronal Microtubule Acetylation by Regulating αTAT1 Degradation. GIP通过调节αTAT1降解影响神经元微管乙酰化。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-02-17 DOI: 10.1002/cm.70107

Beibei Guo, Yan Yue, Xiaoqian Luo, Yao Zhou, Jing Yu, Ximan Yang, Yufang Zhang, Man Xu, Mei Liu, Yan Liu, Tuchen Guan

{"title":"GIP Affects Neuronal Microtubule Acetylation by Regulating αTAT1 Degradation.","authors":"Beibei Guo, Yan Yue, Xiaoqian Luo, Yao Zhou, Jing Yu, Ximan Yang, Yufang Zhang, Man Xu, Mei Liu, Yan Liu, Tuchen Guan","doi":"10.1002/cm.70107","DOIUrl":"https://doi.org/10.1002/cm.70107","url":null,"abstract":"Our understanding of the intrinsic mechanisms that drive the regeneration of damaged axons after a spinal cord injury is still limited. Microtubules are core components of the eukaryotic cytoskeleton and are essential for axonal growth, in part because their stability is governed by post-translational modifications in mature neurons. Glucose-dependent insulinotropic polypeptide (GIP) and its receptor (GIPR) are expressed in multiple extra-pancreatic tissues, suggesting biological functions beyond classical endocrine signaling; however, their roles in neuronal cytoskeletal regulation are not well defined. Here, we investigated the effects of GIP in cultured cortical neurons. GIP enhanced microtubule stability and increased the number of axons crossing an inhibitory chondroitin sulfate proteoglycan (CSPG) border. Mechanistically, GIP promoted microtubule acetylation via α-tubulin N-acetyltransferase 1 (αTAT1), the major acetyltransferase for α-tubulin, by suppressing αTAT1 ubiquitination and thereby reducing its proteasomal degradation in inhibitory environments. Although the upstream mechanism remains to be determined, this study provides the first evidence that GIP/GIPR signaling modulates microtubule dynamics, highlighting a potential strategy to re-activate neuronal growth machinery after injury.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":1.6,"publicationDate":"2026-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146215099","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

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Picture of the Month by Jayne Aiken, Emily Bates, Jeffrey K. Moore, Santos J. Franco, and Mark A. Gutierrez. 本月图片由杰恩·艾肯、艾米丽·贝茨、杰弗里·k·摩尔、桑托斯·j·弗兰科和马克·a·古铁雷斯创作。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-02-11 DOI: 10.1002/cm.70098

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Investigating the Cytoskeleton of DRGs Using Cryo-Electron Microscopy and Deep Learning. 利用冷冻电镜和深度学习技术研究DRGs的细胞骨架。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-02-07 DOI: 10.1002/cm.70100

M Neal Waxham, Mihir Relan, Matthew T Swulius, Andrea K H Stavoe

{"title":"Investigating the Cytoskeleton of DRGs Using Cryo-Electron Microscopy and Deep Learning.","authors":"M Neal Waxham, Mihir Relan, Matthew T Swulius, Andrea K H Stavoe","doi":"10.1002/cm.70100","DOIUrl":"https://doi.org/10.1002/cm.70100","url":null,"abstract":"We describe a method for determining the ultrastructural organization of axons and varicosities of cultured dorsal root ganglion (DRG) neurons using cryogenic electron microscopy (cryo-EM). Cryo-EM reveals the dimensions, proximity, and overall organization of biological specimens in a near-native state, avoiding artifacts of fixation and heavy metal staining employed in classic thin section ultramicroscopy. Cryo-EM excels with thin specimens, and the axons of cryo-preserved cultured DRG neurons are the ideal thickness for high-resolution cryo-electron tomography. DRG neurons are a particularly interesting neuronal preparation because they can be isolated from animals of any age, providing a unique resource to examine age-related changes in axonal morphology. We provide a detailed, step-by-step protocol from DRG isolation and culturing, through cryo-preservation and data acquisition and analysis. We also provide a description for data processing in batch and how implementing deep-learning strategies can facilitate taking tilt-series data through the process of semi-automated tomographic segmentation required for quantitative descriptions of ultrastructural features. We use segmentations focused on the cytoskeletal elements of axons and varicosities of young and old cultured DRG neurons to highlight the approach.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":1.6,"publicationDate":"2026-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146133640","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Expression, Purification, and Microscopy-Based Assays for Engineered Recombinant Tyrosinated, Detyrosinated, and Δ2 Human Tubulin. 工程重组酪氨酸化、去酪氨酸化和Δ2人微管蛋白的表达、纯化和基于显微镜的检测。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-01-07 DOI: 10.1002/cm.70089

Jiayi Chen, Agnieska Szyk, Antonina Roll-Mecak

引用次数: 0