Cytoskeleton (Hoboken, N.J.)最新文献

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Proteomic Mapping of Novel Tubulin Post-Translational Modifications in Trypanosoma cruzi Cytoskeleton. 克氏锥虫细胞骨架中新型微管蛋白翻译后修饰的蛋白质组学定位。
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-10-15 DOI: 10.1002/cm.70211
Gonzalo Martinez Peralta, Daiana Baldelomar, Lucila Baldasseroni, Maria Azul de Hernandez, Esteban Carlos Serra, Victoria Lucía Alonso
{"title":"Proteomic Mapping of Novel Tubulin Post-Translational Modifications in Trypanosoma cruzi Cytoskeleton.","authors":"Gonzalo Martinez Peralta, Daiana Baldelomar, Lucila Baldasseroni, Maria Azul de Hernandez, Esteban Carlos Serra, Victoria Lucía Alonso","doi":"10.1002/cm.70211","DOIUrl":"https://doi.org/10.1002/cm.70211","url":null,"abstract":"<p><p>Microtubules play central roles in the organization and morphology of trypanosomatid parasites, forming highly specialized cytoskeletal structures such as the subpellicular corset, the flagellar axoneme, and the mitotic spindle. Functional specialization of MTs is proposed to be regulated by the \"tubulin code\", which is defined by the combination of different α- and β-tubulin isotypes, a set of post-translational modifications and specific MT-binding proteins. Although multiple tubulin post-translational modifications have been described in trypanosomatids using specific antibodies or mass spectrometry, to date no comprehensive mapping has been reported in Trypanosoma cruzi, the causative agent of Chagas Disease. In the present work, we performed a high-resolution proteomic analysis of PTMs present in α- and β-tubulin subunits of the T. cruzi Dm28c strain, using tubulin-enriched extracts obtained by in vitro polymerization. Multiple high-confidence PTMs were identified by LC-MS/MS, including acetylation, methylation, phosphorylation, and polyglutamylation, for which many modified amino acids had not been previously reported in trypanosomatids. Structural mapping of these modifications onto a predicted α/β-tubulin heterodimer showed that most modified residues are located in solvent-exposed regions of the protein. Together, these findings provide the first high-confidence proteomic landscape of tubulin PTMs in T. cruzi and support the existence of a complex tubulin code contributing to microtubule regulation in this parasite.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"e70211"},"PeriodicalIF":1.6,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149197918","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
KIF1A-Mediated Axonal Transport of Netrin-1 in iPSC-Derived Human Forebrain Neurons. kif1a介导ipsc来源的人前脑神经元Netrin-1的轴突转运。
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-09-26 DOI: 10.1002/cm.70207
T Y Leung, J Sidhu, A Hsieh, Y Ma, J Liu, M A Silverman
{"title":"KIF1A-Mediated Axonal Transport of Netrin-1 in iPSC-Derived Human Forebrain Neurons.","authors":"T Y Leung, J Sidhu, A Hsieh, Y Ma, J Liu, M A Silverman","doi":"10.1002/cm.70207","DOIUrl":"https://doi.org/10.1002/cm.70207","url":null,"abstract":"<p><p>Netrin-1 is a secreted laminin-like protein that functions as a guidance cue for axon pathfinding in development. Netrin-1 also modulates synapse formation in developing neurons and long-term potentiation in mature neurons. Netrin-1 is expressed in human neurons; however, its intracellular distribution and trafficking have not been assessed. Moreover, there is a genetic association in Caenorhabditis elegans between UNC-6/netrin-1 and UNC-104/KIF1A, a kinesin-3 motor protein required for axonal transport. We characterized the endogenous expression of netrin-1 via immunocytochemistry and demonstrated it is localized to both the axon and dendrites of induced pluripotent stem cell (iPSC)-derived human forebrain neurons. Next, live-cell imaging of netrin-1-mRFP revealed rapid, bidirectional axonal transport, comparable to that of other cargos undergoing microtubule-based trafficking in vertebrate neurons. To identify the netrin-1 vesicle population, co-localization analyses demonstrated that netrin-1 puncta overlap with the dense-core vesicle marker Chromogranin A. Netrin-1-mRFP and Chromogranin A-eGFP also undergo co-transport within the axon. Finally, we demonstrated a role for the kinesin-3 motor protein, KIF1A, in Netrin-1 transport by demonstrating that KIF1A-associated neurological disease (KAND) patient variants significantly reduce netrin-1 axonal transport.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"e70207"},"PeriodicalIF":1.6,"publicationDate":"2026-09-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149066529","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
Hot and Splicey: Kinesin Isoforms Seek Attention. 热与粘:运动蛋白异构体寻求关注。
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-09-25 DOI: 10.1002/cm.70208
C Belhadi, M A Silverman
{"title":"Hot and Splicey: Kinesin Isoforms Seek Attention.","authors":"C Belhadi, M A Silverman","doi":"10.1002/cm.70208","DOIUrl":"https://doi.org/10.1002/cm.70208","url":null,"abstract":"<p><p>Kinesins family members (KIFs) are encoded in mammals by approximately 45 genes, which are grouped into 14 families based on structural and functional features. As cells increased in complexity, so too did the demand for specialized kinesin-mediated processes, including intracellular transport, cytoskeletal organization, and cell division. One mechanism driving this diversity is alternative splicing, which can generate multiple protein isoforms with distinct properties. Here, we highlight examples of KIF isoforms that differ in cargo binding and biophysical motor behavior, as well as their roles in cell cycle regulation, development, and cancer. Moreover, using the HUGO and UniProt databases, we select a few KIF isoforms and propose functional implications based on sequence alterations from that of the canonical transcript and protein. Given that isoform-specific functional differences may have important consequences, we emphasize the need for future studies to investigate kinesin isoforms to better understand their roles in cellular processes and disease.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"e70208"},"PeriodicalIF":1.6,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149042303","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
The I130V and S229F Tropomyosin Mutations Associated With Congenital Heart Disease Disrupt Actin-Myosin Interactions in the Atria. 与先天性心脏病相关的原肌球蛋白I130V和S229F突变破坏心房肌动蛋白-肌球蛋白相互作用
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-09-22 DOI: 10.1002/cm.70206
Galina V Kopylova, Anastasia M Kochurova, Andrey V Slushchev, Daria S Yampolskaya, Julia Y Antonets, Natalia S Ryabkova, Ivan A Katrukha, Sergey Y Kleymenov, Sergey Y Bershitsky, Alexander M Matyushenko, Dmitrii I Levitsky, Daniil V Shchepkin
{"title":"The I130V and S229F Tropomyosin Mutations Associated With Congenital Heart Disease Disrupt Actin-Myosin Interactions in the Atria.","authors":"Galina V Kopylova, Anastasia M Kochurova, Andrey V Slushchev, Daria S Yampolskaya, Julia Y Antonets, Natalia S Ryabkova, Ivan A Katrukha, Sergey Y Kleymenov, Sergey Y Bershitsky, Alexander M Matyushenko, Dmitrii I Levitsky, Daniil V Shchepkin","doi":"10.1002/cm.70206","DOIUrl":"https://doi.org/10.1002/cm.70206","url":null,"abstract":"<p><p>Tropomyosin is a highly conserved α-helical coiled-coil protein that is involved in maintaining the structural integrity of the sarcomere and regulating contraction of striated muscle. Mutations in the TPM1 gene encoding cardiac α-tropomyosin (Tpm1.1) are associated with left ventricular noncompact cardiomyopathy and congenital heart defects (CHD). We investigated the structural and functional properties of Tpm1.1 with the I130V and S229F mutations associated with CHD. We found that both mutations decreased the Tpm affinity for F-actin and differently affected the sliding velocity of F-actin-Tpm filaments over ventricular and atrial myosin in an in vitro motility assay. The results indicate a disruption in the activation of F-actin-Tpm filaments by myosin cross-bridges with both atrial and ventricular myosin. The I130V mutation increased the maximum sliding velocity of thin filaments over atrial myosin and decreased the Ca<sup>2+</sup> sensitivity of the filament velocity. The S229F mutation increased the maximum filament velocity on atrial myosin and decreased the Hill coefficient. The mutations did not affect the Ca<sup>2+</sup>-dependent characteristics of thin filament velocity with ventricular myosin. Thus, the molecular mechanism of CHD pathogenesis induced by Tpm1.1 mutations is associated with changes in sarcomere stability and disruption of actin-myosin interaction in the myocardium of the ventricles and atria, which negatively affect the contractility of both heart chambers.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"e70206"},"PeriodicalIF":1.6,"publicationDate":"2026-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149018905","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
Quantifying Actin Persistence Length in S. pombe and S. cerevisiae: The Impact of Data Size, Filament Length and Fitting Strategy. 量化pombe和cerevisiae的肌动蛋白持续长度:数据大小、丝长和拟合策略的影响。
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-09-21 DOI: 10.1002/cm.70193
Peter Nietmann, Andrejus Suchenko, Andreas Janshoff, Mohan K Balasubramanian
{"title":"Quantifying Actin Persistence Length in S. pombe and S. cerevisiae: The Impact of Data Size, Filament Length and Fitting Strategy.","authors":"Peter Nietmann, Andrejus Suchenko, Andreas Janshoff, Mohan K Balasubramanian","doi":"10.1002/cm.70193","DOIUrl":"https://doi.org/10.1002/cm.70193","url":null,"abstract":"<p><p>Actin filaments exhibit isoform and species-specific mechanical properties that are commonly quantified via their persistence length, yet the reliability of such measurements depends not only on the analysis method but also on dataset characteristics. Here, we measure and compare the persistence lengths of actin filaments from Schizosaccharomyces pombe and Saccharomyces cerevisiae as two exemplars, focusing on statistical and methodological factors that influence their determination. We evaluate common cosine-correlation-based analysis strategies and systematically assess the impact of filament length and dataset size on the accuracy of extracted persistence lengths. Because the bending stiffness of actin filaments can scale non-linearly with filament numbers in bundles, even small errors in the persistence length can have disproportionately large impact on the estimation of mechanical behavior. We validate our findings through comparative analysis utilizing simulated thermal fluctuations of semi-flexible polymers. Our results reinforce the importance of filament length and dataset size for the reliability of persistence length estimation, suggesting that their influence may have been underestimated. We introduce a weighting strategy that reduces the influence of error-dominated correlation regimes and improves the robustness of the analysis. This work contributes a quantitative framework for designing experiments and analyzing actin filament mechanics, ensuring robust and reproducible persistence length measurements. Furthermore, applying this approach revealed a significant difference in the persistence lengths of S. pombe and S. cerevisiae actin filaments.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"e70193"},"PeriodicalIF":1.6,"publicationDate":"2026-09-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149013393","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
Pathogenic Bordetella Bacteria Exploit Axonemal Microtubules to Penetrate the Ciliary Barrier. 致病性博氏杆菌利用轴突微管穿透睫状体屏障。
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-09-21 DOI: 10.1002/cm.70205
Michael S Costello, Mia W Raimondi, Christopher S Hayes
{"title":"Pathogenic Bordetella Bacteria Exploit Axonemal Microtubules to Penetrate the Ciliary Barrier.","authors":"Michael S Costello, Mia W Raimondi, Christopher S Hayes","doi":"10.1002/cm.70205","DOIUrl":"10.1002/cm.70205","url":null,"abstract":"<p><p>Respiratory pathogens face a daunting physical challenge during host colonization. Invading microbes must resist elimination by motile respiratory cilia, which beat continuously to sweep debris from the airways. Bacteria have long been known to use adhesive proteins to bind host cells, but recent work shows that Bordetella species utilize an unusual strategy to colonize respiratory epithelia. Bordetella deploy FhaB adhesins that translocate a novel microtubule-binding domain into cilia to interact with the axoneme. These findings reveal FhaB to be a unique adhesive factor that exploits the internal cytoskeleton to colonize a protected niche in the host respiratory tract.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"e70205"},"PeriodicalIF":1.6,"publicationDate":"2026-09-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13653760/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149013369","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
Increased Insulin Action, Glucose Metabolism and Muscle Function in Supervillin-Knockout and Supervillin-Mutant Mice. 超级绒毛蛋白敲除和突变小鼠胰岛素作用、葡萄糖代谢和肌肉功能的增加。
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-09-16 DOI: 10.1002/cm.70196
Tara C Smith, Lauren A Tauer, Randall H Friedline, Xiaodi Hu, Duy Tran, Yangyi E Luo, Nacima Hadjout-Rabi, Elisabeth R Barton, Jason K Kim, Elizabeth J Luna
{"title":"Increased Insulin Action, Glucose Metabolism and Muscle Function in Supervillin-Knockout and Supervillin-Mutant Mice.","authors":"Tara C Smith, Lauren A Tauer, Randall H Friedline, Xiaodi Hu, Duy Tran, Yangyi E Luo, Nacima Hadjout-Rabi, Elisabeth R Barton, Jason K Kim, Elizabeth J Luna","doi":"10.1002/cm.70196","DOIUrl":"https://doi.org/10.1002/cm.70196","url":null,"abstract":"<p><p>We here describe mouse models with complementary homozygous Svil mutations. In skeletal muscle, Svil-Mut mice express the Svil-encoded N-terminus fused to the βgal-neo gene-trap tag and lack the highly conserved archvillin C-terminus; Svil-KO mice lack expression of all known Svil-encoded proteins; and Svil-LoxP mice contain loxP sites for tissue-specific disruption of protein expression. Older Svil-KO male mice showed decreased levels of markers for type 1, 2a, and 2b muscle fibers. Male mice showed elevated P-ERK/ERK signaling during lengthening contractions, consistent with low-level muscle damage such as that in myofibrillar myopathy-10 (MFM10) in humans lacking SVIL proteins. Female mice lacking full-length Svil-encoded proteins, including supervillin and archvillin, exhibited reduced body weights and reduced fat mass. Females in both strains exhibited improved glucose tolerance and lower insulin levels following intraperitoneal glucose injections. Hyperinsulinemic-euglycemic clamp experiments showed increased insulin sensitivity in both strains and increased glucose metabolism in adipose tissues in female Svil-Mut mice. The GLUT4 glucose transporter was increased in skeletal muscle in breeder-aged female Svil-KO and Svil-Mut mice. RNA-Seq revealed transcriptional differences in adult male homeostatic muscles that supported roles in muscle differentiation, ERK signaling, and lipid metabolism. A yeast two-hybrid screen identified new Svil candidate interactors, including CH1 domains of muscle Z-line proteins, a potential dimerization site, and Rho GTPase-activating protein (ARHGAP21), a negative regulator of glucose-stimulated insulin secretion in pancreatic beta cells. We suggest that the Svil-Mut, Svil-KO, and Svil-LoxP strains described here will be useful models for understanding signaling within and between tissues regulating glucose metabolism.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":1.6,"publicationDate":"2026-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148978645","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
Hyperactive KIF5A in Neurodegeneration. 神经退行性疾病中KIF5A过度活跃。
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-09-14 DOI: 10.1002/cm.70204
David Villarroel-Campos, James N Sleigh
{"title":"Hyperactive KIF5A in Neurodegeneration.","authors":"David Villarroel-Campos, James N Sleigh","doi":"10.1002/cm.70204","DOIUrl":"https://doi.org/10.1002/cm.70204","url":null,"abstract":"<p><p>The highly polarised morphology of neurons and the sheer length of their axons make transport of cargoes throughout the cell a formidable task. Decades of evidence obtained from genetic studies on patients and animal models highlight deficits in axonal transport as a recurrent cause, or early contributing factor, in a plethora of neurodegenerative diseases. Axonal transport abnormalities usually manifest as a slowing of cargo trafficked by molecular motors along microtubules; however, hyperactivation of motors can also lead to disease. That is the case for the kinesin-1 protein KIF5A, in which hyperactive mutations are linked to amyotrophic lateral sclerosis (ALS) and neonatal intractable myoclonus (NEIMY). In this Perspective, we summarise the latest insights into the impact of KIF5A hyperactivity, such as loss of autoinhibition, aggregation, altered cargo binding and microtubule damage. We conclude by discussing possible strategies to counteract these disruptions, with an emphasis on the necessity of restoring axonal transport to physiological levels, a key requirement to maintain neuronal homeostasis.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"e70204"},"PeriodicalIF":1.6,"publicationDate":"2026-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148964037","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
Author Profile. 作者概要文件。
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-09-14 DOI: 10.1002/cm.70191
Purva Khodke
{"title":"Author Profile.","authors":"Purva Khodke","doi":"10.1002/cm.70191","DOIUrl":"https://doi.org/10.1002/cm.70191","url":null,"abstract":"","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"e70191"},"PeriodicalIF":1.6,"publicationDate":"2026-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148964018","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
New Insights Into the Three-Dimensional Mechanics of the Flagellar Beat Cycle. 鞭毛跳动周期的三维力学新见解。
IF 1.6
Cytoskeleton (Hoboken, N.J.) Pub Date : 2026-09-12 DOI: 10.1002/cm.70203
Charles B Lindemann
{"title":"New Insights Into the Three-Dimensional Mechanics of the Flagellar Beat Cycle.","authors":"Charles B Lindemann","doi":"10.1002/cm.70203","DOIUrl":"https://doi.org/10.1002/cm.70203","url":null,"abstract":"<p><p>Advances in imaging at the molecular scale have provided greater detail concerning the three-dimensional structure of the ciliary/flagellar axoneme. Additionally, it has recently been confirmed that electrostatic forces regulate the dynein-tubulin interaction at the microtubule binding domain (MTBD) of dynein, and at the junction of the nexin-dynein regulatory complex (N-DRC) with the adjacent outer doublet. There is also considerable evidence that radial spokes (RSs) and the central pair (CP) apparatus primarily contribute to the mechanical functioning of the axoneme. These discoveries make it possible to analyze in more detail how stresses are transferred within the three-dimensional axoneme structure. This report evaluates how stress that is generated when the axoneme bends is distributed to the various structural components. Based on the latest findings, it appears that transverse stress generated during active beating is primarily distributed to the N-DRC and the MTBDs of the dynein heavy chains. It is the balance of tension between the N-DRC and inner dynein arms (IDAs) that is the key regulator of dynein switching in the beat cycle. The stress distribution to the IDAs impacts the functioning of the dynein heavy chains by inhibition of stepping. This analysis supports a key tenet of the Geometric Clutch (GC) hypothesis of flagellar beating.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":"e70203"},"PeriodicalIF":1.6,"publicationDate":"2026-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148957417","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
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