{"title":"Myosin-induced F-actin fragmentation facilitates contraction of actin networks","authors":"Kyohei Matsuda, Wonyeong Jung, Yusei Sato, Takuya Kobayashi, Masahiko Yamagishi, Taeyoon Kim, Junichiro Yajima","doi":"10.1002/cm.21848","DOIUrl":"10.1002/cm.21848","url":null,"abstract":"<p>Mechanical forces play a crucial role in diverse physiological processes, such as cell migration, cytokinesis, and morphogenesis. The actin cytoskeleton generates a large fraction of the mechanical forces via molecular interactions between actin filaments (F-actins) and myosin motors. Recent studies have shown that the common tendency of actomyosin networks to contract into a smaller structure deeply involves F-actin buckling induced by motor activities, fragmentation of F-actins, and the force-dependent unbinding of cross-linkers that inter-connect F-actins. The fragmentation of F-actins was shown to originate from either buckling or tensile force from previous single-molecule experiments. While the role of buckling in network contraction has been studied extensively, to date, the role of tension-induced F-actin fragmentation in network contraction has not been investigated. In this study, we employed in vitro experiments and an agent-based computational model to illuminate when and how the tension-induced F-actin fragmentation facilitates network contraction. Our experiments demonstrated that F-actins can be fragmented due to tensile forces, immediately followed by catastrophic rupture and contraction of networks. Using the agent-based model, we showed that F-actin fragmentation by tension results in distinct rupture dynamics different from that observed in networks only with cross-linker unbinding. Moreover, we found that tension-induced F-actin fragmentation is particularly important for the contraction of networks with high connectivity. Results from our study shed light on an important regulator of the contraction of actomyosin networks which has been neglected. In addition, our results provide insights into the rupture mechanisms of polymeric network structures and bio-inspired materials.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 8","pages":"339-355"},"PeriodicalIF":2.4,"publicationDate":"2024-03-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21848","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140061397","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
CytoskeletonPub Date : 2024-03-07DOI: 10.1002/cm.21849
Vitaly Zimyanin, Stefanie Redemann
{"title":"Microtubule length correlates with spindle length in C. elegans meiosis","authors":"Vitaly Zimyanin, Stefanie Redemann","doi":"10.1002/cm.21849","DOIUrl":"10.1002/cm.21849","url":null,"abstract":"<p>The accurate segregation of chromosomes during female meiosis relies on the precise assembly and function of the meiotic spindle, a dynamic structure primarily composed of microtubules. Despite the crucial role of microtubule dynamics in this process, the relationship between microtubule length and spindle size remains elusive. Leveraging <i>Caenorhabditis elegans</i> as a model system, we combined electron tomography and live imaging to investigate this correlation. Our analysis revealed significant changes in spindle length throughout meiosis, coupled with alterations in microtubule length. Surprisingly, while spindle size decreases during the initial stages of anaphase, the size of antiparallel microtubule overlap decreased as well. Detailed electron tomography shows a positive correlation between microtubule length and spindle size, indicating a role of microtubule length in determining spindle dimensions. Notably, microtubule numbers displayed no significant association with spindle length, highlighting the dominance of microtubule length regulation in spindle size determination. Depletion of the microtubule depolymerase KLP-7 led to elongated metaphase spindles with increased microtubule length, supporting the link between microtubule length and spindle size. These findings underscore the pivotal role of regulating microtubule dynamics, and thus microtubule length, in governing spindle rearrangements during meiotic division, shedding light on fundamental mechanisms dictating spindle architecture.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 8","pages":"356-368"},"PeriodicalIF":2.4,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21849","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140051235","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Temperature-dependent augmentation of ciliary motility by the TRP2 channel in Chlamydomonas reinhardtii","authors":"Shunta Fueki, Taro Kaneko, Haruka Matsuki, Yuki Hashimoto, Megumi Yoshida, Atsuko Isu, Ken-ichi Wakabayashi, Kenjiro Yoshimura","doi":"10.1002/cm.21840","DOIUrl":"10.1002/cm.21840","url":null,"abstract":"<p>Temperature is a critical factor for living organisms. Many microorganisms migrate toward preferable temperatures, and this behavior is called thermotaxis. In this study, the molecular and physiological bases for thermotaxis are examined in <i>Chlamydomonas reinhardtii</i>. A mutant with knockout of a transient receptor potential (TRP) channel, <i>trp2-3</i>, showed defective thermotaxis. The swimming velocity and ciliary beat frequency of wild-type <i>Chlamydomonas</i> increase with temperature; however, this temperature-dependent enhancement of motility was almost absent in the <i>trp2-3</i> mutant. Wild-type <i>Chlamydomonas</i> showed negative thermotaxis, but mutants deficient in the outer or inner dynein arm showed positive thermotaxis and a defect in temperature-dependent increase in swimming velocity, suggesting involvement of both dynein arms in thermotaxis.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 11","pages":"578-585"},"PeriodicalIF":2.4,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21840","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139998488","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The ability of the LIMD1 and TRIP6 LIM domains to bind strained f-actin is critical for their tension dependent localization to adherens junctions and association with the Hippo pathway kinase LATS1","authors":"Samriddha Ray, Chamika DeSilva, Ishani Dasgupta, Sebastian Mana-Capelli, Natasha Cruz-Calderon, Dannel McCollum","doi":"10.1002/cm.21847","DOIUrl":"10.1002/cm.21847","url":null,"abstract":"<p>A key step in regulation of Hippo pathway signaling in response to mechanical tension is recruitment of the LIM domain proteins TRIP6 and LIMD1 to adherens junctions. Mechanical tension also triggers TRIP6 and LIMD1 to bind and inhibit the Hippo pathway kinase LATS1. How TRIP6 and LIMD1 are recruited to adherens junctions in response to tension is not clear, but previous studies suggested that they could be regulated by the known mechanosensory proteins α-catenin and vinculin at adherens junctions. We found that the three LIM domains of TRIP6 and LIMD1 are necessary and sufficient for tension-dependent localization to adherens junctions. The LIM domains of TRIP6, LIMD1, and certain other LIM domain proteins have been shown to bind to actin networks under strain/tension. Consistent with this, we show that TRIP6 and LIMD1 colocalize with the ends of actin fibers at adherens junctions. Point mutations in a key conserved residue in each LIM domain that are predicted to impair binding to f-actin under strain inhibits TRIP6 and LIMD1 localization to adherens junctions and their ability to bind to and recruit LATS1 to adherens junctions. Together these results show that the ability of TRIP6 and LIMD1 to bind to strained actin underlies their ability to localize to adherens junctions and regulate LATS1 in response to mechanical tension.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 9-10","pages":"436-447"},"PeriodicalIF":2.4,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139998489","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Metastasis-associated 1 localizes to the sarcomeric Z-disc and is implicated in skeletal muscle pathology","authors":"Hongsheng Xue, Li Han, Haidi Sun, Zhe Piao, Wenjun Cao, Haili Qian, Zhilong Zhao, Ming-Fei Lang, Chundong Gu","doi":"10.1002/cm.21841","DOIUrl":"10.1002/cm.21841","url":null,"abstract":"<p>Metastasis-associated 1 (MTA1), a subunit of the nucleosome remodeling and histone deacetylation (NuRD) corepressor complex, was reported to be expressed in the cytoplasm of skeletal muscles. However, the exact subcellular localization and the functional implications of MTA1 in skeletal muscles have not been examined. This study aims to demonstrate the subcellular localization of MTA1 in skeletal muscles and reveal its possible roles in skeletal muscle pathogenesis. Striated muscles (skeletal and cardiac) from C57BL/6 mice of 4–5 weeks were collected to examine the expression of MTA1 by Western blotting and immunohistochemistry. Immunofluorescence and immunoelectron microscopy were performed for MTA1, α-actinin (a Z-disc marker protein), and SMN (survival of motor neuron) proteins. Gene Expression Omnibus (GEO) data sets were analyzed using the GEO2R online tool to explore the functional implications of MTA1 in skeletal muscles. MTA1 expression was detected by Western blotting and immunohistochemistry in skeletal and cardiac muscles. Subcellular localization of MTA1 was found in the Z-disc of sarcomeres, where α-actinin and SMN were expressed. Data mining of GEO profiles suggested that MTA1 dysregulation is associated with multiple skeletal muscle defects, such as Duchenne muscular dystrophy, Emery-Dreifuss muscular dystrophy, nemaline myopathy, and dermatomyositis. The GEO analysis also showed that MTA1 expression gradually decreased with age in mouse skeletal muscle precursor cells. The subcellular localization of MTA1 in sarcomeres of skeletal muscles implies its biological roles in sarcomere structures and its possible contribution to skeletal muscle pathology.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 9-10","pages":"427-435"},"PeriodicalIF":2.4,"publicationDate":"2024-02-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139934552","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
CytoskeletonPub Date : 2024-02-22DOI: 10.1002/cm.21839
Prashali Chauhan, Hong Beom Lee, Niaz Goodbee, Sophia Martin, Ruell Branch, Sumon Sahu, Jennifer M. Schwarz, Jennifer L. Ross
{"title":"Ionic strength alters crosslinker-driven self-organization of microtubules","authors":"Prashali Chauhan, Hong Beom Lee, Niaz Goodbee, Sophia Martin, Ruell Branch, Sumon Sahu, Jennifer M. Schwarz, Jennifer L. Ross","doi":"10.1002/cm.21839","DOIUrl":"10.1002/cm.21839","url":null,"abstract":"<p>The microtubule cytoskeleton is a major structural element inside cells that directs self-organization using microtubule-associated proteins and motors. It has been shown that finite-sized, spindle-like microtubule organizations, called “tactoids,” can form in vitro spontaneously from mixtures of tubulin and the antiparallel crosslinker, MAP65, from the MAP65/PRC1/Ase family. Here, we probe the ability of MAP65 to form tactoids as a function of the ionic strength of the buffer to attempt to break the electrostatic interactions binding MAP65 to microtubules and inter-MAP65 binding. We observe that, with increasing monovalent salts, the organizations change from finite tactoids to unbounded length bundles, yet the MAP65 binding and crosslinking appear to stay intact. We further explore the effects of ionic strength on the dissociation constant of MAP65 using both microtubule pelleting and single-molecule binding assays. We find that salt can reduce the binding, yet salt never negates it. Instead, we believe that the salt is affecting the ability of the MAP65 to form phase-separated droplets, which cause the nucleation and growth of tactoids, as recently demonstrated.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 8","pages":"328-338"},"PeriodicalIF":2.4,"publicationDate":"2024-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21839","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139934551","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
CytoskeletonPub Date : 2024-02-13DOI: 10.1002/cm.21842
{"title":"Front Cover Image","authors":"","doi":"10.1002/cm.21842","DOIUrl":"https://doi.org/10.1002/cm.21842","url":null,"abstract":"<p>ON THE FRONT COVER: Image of the myocardium. Microtubules (cyan), titin (magenta), and the nuclei (yellow) are fluorescently labeled and visualized by confocal microscopy.</p><p>Credit: Andreas Unger and Wolfgang A. Linke, Institute of Physiology II, University Hospital, Münster, Germany\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure>\u0000 </p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 2-3","pages":"C1"},"PeriodicalIF":2.9,"publicationDate":"2024-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21842","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139727774","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
CytoskeletonPub Date : 2024-02-13DOI: 10.1002/cm.21843
{"title":"Inner Front Cover Image","authors":"","doi":"10.1002/cm.21843","DOIUrl":"https://doi.org/10.1002/cm.21843","url":null,"abstract":"<p>ON THE INNER FRONT COVER: A molecular surface representation depicting Chlamydomonas non-conventional actin NAP1 (orange) with the actin depolymerization drug latrunculin-A (light blue spheres) and ATP (gray sticks).</p><p>Credit: Rikuri Morita, University of Tsukuba\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure>\u0000 </p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 2-3","pages":"C2"},"PeriodicalIF":2.9,"publicationDate":"2024-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21843","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139727775","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
CytoskeletonPub Date : 2024-02-13DOI: 10.1002/cm.21845
{"title":"Back Cover Image","authors":"","doi":"10.1002/cm.21845","DOIUrl":"https://doi.org/10.1002/cm.21845","url":null,"abstract":"<p>ON THE BACK COVER: CLIK-1 (shown in green) is a calponin-related actin-binding protein that is predominantly expressed in the body wall muscle of the nematode <i>Caenorhabditis elegans</i>. Overlaps between CLIK-1 and actin filaments (shown in magenta) generate the whitish green appearance of the sarcomeres.</p><p>Credit: Shoichiro Ono, Winship Cancer Institute, Emory University School of Medicine\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure>\u0000 </p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 2-3","pages":"C4"},"PeriodicalIF":2.9,"publicationDate":"2024-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21845","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139727773","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
CytoskeletonPub Date : 2024-02-13DOI: 10.1002/cm.21844
{"title":"Inner Back Cover Image","authors":"","doi":"10.1002/cm.21844","DOIUrl":"https://doi.org/10.1002/cm.21844","url":null,"abstract":"<p>ON THE INNER BACK COVER: With liquid crystal polarized light microscopy, spindle microtubules exhibit striking birefringence, which is color enhanced using the ‘Red Hot’ lookup table in Image J software. This flattened spermatocyte failed to divide after meiosis I and now has both of the two spindles for meiosis II in its lone cytoplasmic space.</p><p>Credit: James LaFountain (University at Buffalo) and Rudolf Oldenbourg (Marine Biological Laboratory)\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure>\u0000 </p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 2-3","pages":"C3"},"PeriodicalIF":2.9,"publicationDate":"2024-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21844","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139727772","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}