Cytoskeleton (Hoboken, N.J.)最新文献_第8页

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

LamelliQuant: An Automated Analysis Pipeline for Lamellipodia Protrusion Dynamics. LamelliQuant：板足突出动力学的自动分析管道。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-01-05 DOI: 10.1002/cm.70094

Ian Eder, Abrahim Kashkoush, Partha Roy

引用次数: 0

Cytoskeleton Spotlight: Michaela Horger. 细胞骨架聚焦：Michaela Horger。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2025-12-22 DOI: 10.1002/cm.70090

Michaela Horger

引用次数: 0

In Vivo Cytoskeletal AMPA Receptor Transport Imaging in C. elegans. 秀丽隐杆线虫体内细胞骨架AMPA受体转运成像。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2025-12-09 DOI: 10.1002/cm.70078

Michaelis A K, Hoerndli F J

{"title":"In Vivo Cytoskeletal AMPA Receptor Transport Imaging in C. elegans.","authors":"Michaelis A K, Hoerndli F J","doi":"10.1002/cm.70078","DOIUrl":"https://doi.org/10.1002/cm.70078","url":null,"abstract":"Long-distance intracellular transport of ionotropic glutamate receptors (iGluRs) is essential for proper excitatory synaptic function underlying learning and memory. Many neuropsychiatric and neurodegenerative conditions have abnormal iGluR transport and trafficking, leading to an intense interest in the mechanisms and factors regulating these processes. Although iGluRs and synaptic protein transport have been studied in cultured neurons, in vitro systems lack the specific connectivity of native circuits essential for the organization and regulation of compartmentalized synaptic signaling. Here, we describe an in vivo imaging approach that leverages the optical transparency of C. elegans to measure the transport of glutamate receptors in a fully intact neural system. Our workflow includes a standardized protocol for worm mounting, high-resolution imaging, and quantification of motor-driven iGluR transport in C. elegans. We discuss critical parameters for optimal signal-to-noise ratio, analysis, and reproducibility. Through years of optimization, we have established which fluorophores and genetic tools are the most effective and reproducible for in vivo transport imaging. These results provide a refined and reproducible framework for studying motor-driven iGluR transport in an intact nervous system and highlight important technical variables that can affect in vivo transport imaging.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":1.6,"publicationDate":"2025-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145709931","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

Protocol for Reconstituting Adaptor-Mediated Activation of Full-Length Kinesin-1. 重组接头介导的全长激酶-1激活的方案。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2025-12-05 DOI: 10.1002/cm.70079

Haruka Masumoto, Kyoko Chiba

{"title":"Protocol for Reconstituting Adaptor-Mediated Activation of Full-Length Kinesin-1.","authors":"Haruka Masumoto, Kyoko Chiba","doi":"10.1002/cm.70079","DOIUrl":"https://doi.org/10.1002/cm.70079","url":null,"abstract":"Kinesin-1 is a member of the kinesin superfamily that plays an essential role in intracellular cargo transport. In the absence of cargo, Kinesin-1 exhibits low motor activity due to autoinhibition. Multiple studies have demonstrated that adaptor proteins, which link cargos to Kinesin-1, can activate Kinesin-1 by releasing the autoinhibition. To elucidate the molecular mechanism of adaptor-mediated activation, in vitro reconstitution of the Kinesin-1 complex has proven to be a powerful approach. We have shown that the binding of an adaptor protein, Nesprin-4, is sufficient to activate Kinesin-1 motility in vitro. Here, we present protocols for the observation and assessment of adaptor-mediated Kinesin-1 activation. Using C. elegans and human Kinesin-1 as examples, we describe steps and critical considerations for preparing the Kinesin-1 complex. We also detail how to mix it with an adaptor protein and visualize the resulting motility using total internal reflection fluorescence (TIRF) microscopy. Finally, we describe analytical methods for assessing motor activation. This protocol will be valuable for future studies aiming to evaluate the activation of Kinesin-1 by known or unknown activator molecules.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":1.6,"publicationDate":"2025-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145679563","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

Isoform Specificity of a Compound Targeting Actin Filaments Containing Tropomyosin Tpm1.8/1.9. 一种靶向含有原肌球蛋白Tpm1.8/1.9的肌动蛋白细丝的化合物的异构体特异性

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2025-10-14 DOI: 10.1002/cm.70055

Jeff Hook, Edna C Hardeman, Peter W Gunning

{"title":"Isoform Specificity of a Compound Targeting Actin Filaments Containing Tropomyosin Tpm1.8/1.9.","authors":"Jeff Hook, Edna C Hardeman, Peter W Gunning","doi":"10.1002/cm.70055","DOIUrl":"https://doi.org/10.1002/cm.70055","url":null,"abstract":"The unbranched actin filaments in mammalian cells are usually composed of co-polymers of a specific tropomyosin isoform with actin. Genetic manipulation has revealed that the tropomyosins largely define the functional properties of actin filaments in an isoform-specific, non-redundant manner. Tropomyosin isoforms play a role in human diseases including cancers, thrombocytopenia and thrombocythaemia, endometrial decidualisation resistance, and ulcerative colitis. Hence, the development of compounds that target different tropomyosins are potentially valuable tools for cell biology as well as potential therapeutics. We have recently identified compounds that target Tpm1.8/1.9 and now address the isoform specificity of these compounds. Tpm1.8/1.9 is primarily enriched in the lamellipodium of migrating cells but not in stress fibre bundles unlike Tpm3.1/3.2 and Tpm4.2, which are enriched in stress fibres. Human fibroblasts also incorporate Tpm1.8/1.9 into fine filaments emanating from the perinuclear region. Exposure of human fibroblasts and SK-N-SH cells to the compounds 189-1 and 189-3 results in dispersal of Tpm1.8/1.9 from the lamellipodium and fine filaments to a diffuse organisation in the cytoplasm. In contrast, at doses that disperse Tpm1.8/1.9, 189-3 has no impact on the association of either Tpm3.1/3.2 or Tpm4.2 with actin filament bundles, whereas 189-1 also targets Tpm4.2. Tpm1.8/1.9 organisation becomes dispersed between 12- and 18-hour exposure to 189-3, and the organisation of Tpm1.8/1.9 returns within 4 h of drug washout. We conclude that the amino acid sequence differences located at 7 positions in the first 19 residues of these isoforms provide sufficient specificity to generate compounds that target Tpm1.8/1.9 alone.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":1.6,"publicationDate":"2025-10-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145287914","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

Picture of the Month by Prabhat Tiwari and Erika Geisbrecht. 月之图由Prabhat Tiwari和Erika Geisbrecht创作。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2025-09-15 DOI: 10.1002/cm.70043

引用次数: 0

Correction to "The Mechanics of Cilia and Flagella: What We Know and What We Need to Know". 更正“纤毛和鞭毛的机制：我们知道什么和我们需要知道什么”。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2025-08-01 Epub Date: 2025-02-14 DOI: 10.1002/cm.22003

引用次数: 0

End Binding Proteins: Drivers of Cancer Progression. 末端结合蛋白：癌症进展的驱动因素。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2025-08-01 Epub Date: 2024-12-19 DOI: 10.1002/cm.21972

Dhakshmi Sasankan, Renu Mohan

{"title":"End Binding Proteins: Drivers of Cancer Progression.","authors":"Dhakshmi Sasankan, Renu Mohan","doi":"10.1002/cm.21972","DOIUrl":"10.1002/cm.21972","url":null,"abstract":"Cancer, a complex and heterogeneous disease, continues to be a major global health concern. Despite advancements in diagnostics and therapeutics, the aggressive nature of certain cancers remain a significant challenge, necessitating a deeper understanding of the underlying molecular mechanisms driving their severity and progression. Cancer severity and progression depend on cellular properties such as cell migration, cell division, cell shape changes, and intracellular transport, all of which are driven by dynamic cellular microtubules. Dynamic properties of microtubules, in turn, are regulated by an array of proteins that influence their stability and growth. Among these regulators, End Binding (EB) proteins stand out as critical orchestrators of microtubule dynamics at their growing plus ends. Beyond their fundamental role in normal cellular functions, recent research has uncovered compelling evidence linking EB proteins to the pathogenesis of various diseases, including cancer progression. As the field of cancer research advances, the clinical implication of EB proteins role in cancer severity and aggressiveness become increasingly evident. This review aims to comprehensively explore the role of microtubule-associated EB proteins in influencing the severity and aggressiveness of cancer. We also discuss the potential significance of EB as a clinical biomarker for cancer diagnosis and prognosis and as a target for therapeutic intervention.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"483-496"},"PeriodicalIF":1.6,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142856906","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

Overexpressed Palladin Rescues Enteropathogenic E. coli (EPEC) Pedestal Lengths in ArpC2 Depleted Cells. 在ArpC2缺失的细胞中，过表达的Palladin可挽救肠致病性大肠杆菌（EPEC）基座长度。

IF 1.6

Cytoskeleton (Hoboken, N.J.) Pub Date : 2025-08-01 Epub Date: 2024-12-18 DOI: 10.1002/cm.21974

Kaitlin M Bruzzini, S Tara Mann, Julian A Guttman

{"title":"Overexpressed Palladin Rescues Enteropathogenic E. coli (EPEC) Pedestal Lengths in ArpC2 Depleted Cells.","authors":"Kaitlin M Bruzzini, S Tara Mann, Julian A Guttman","doi":"10.1002/cm.21974","DOIUrl":"10.1002/cm.21974","url":null,"abstract":"Enteropathogenic Escherichia coli (EPEC) causes diarrheal disease. Once ingested, these extracellular pathogens attach to the intestinal epithelial cells of their host, collapse the localized microvilli, and generate actin-rich structures within the host cells that are located beneath the attached bacteria, called \"pedestals.\" Palladin is an actin-associated protein that cross-links and stabilizes actin filaments. This protein also acts as a scaffolding protein for other actin-binding proteins. Here, we examine the role of Palladin during EPEC infections and show that Palladin is co-opted by EPEC. Depletion of Palladin resulted in shorter pedestals, and when Palladin containing mutations in either its actin- or VASP-binding domains were overexpressed in cells, pedestals decreased in length. Importantly, we show that the overexpression of Palladin in ArpC2 -/- (Arp2/3 complex-depleted) cells rescued pedestal length. Together, our results demonstrate that Palladin has the ability to rescue pedestal length during EPEC infections when the function of the Arp2/3 complex is diminished.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"497-512"},"PeriodicalIF":1.6,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12330885/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142848445","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0