Cytoskeleton最新文献

{"title":"A special issue on the physics of the cytoskeleton","authors":"Dimitrios Vavylonis, Allen P. Liu, Yuan-Nan Young","doi":"10.1002/cm.21902","DOIUrl":"10.1002/cm.21902","url":null,"abstract":"","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 8","pages":"295-296"},"PeriodicalIF":2.4,"publicationDate":"2024-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141914705","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":"Author profile: Dr. Samriddha Ray","authors":"Samriddha Ray","doi":"10.1002/cm.21900","DOIUrl":"10.1002/cm.21900","url":null,"abstract":"","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 9-10","pages":"500-501"},"PeriodicalIF":2.4,"publicationDate":"2024-08-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141908519","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":"Author profile","authors":"Aparna Bhattacharyya","doi":"10.1002/cm.21903","DOIUrl":"10.1002/cm.21903","url":null,"abstract":"","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 9-10","pages":"502-503"},"PeriodicalIF":2.4,"publicationDate":"2024-08-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141908518","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":"Comparative structural study on axonemal and cytoplasmic dyneins","authors":"Noemi Zimmermann,&nbsp;Takashi Ishikawa","doi":"10.1002/cm.21897","DOIUrl":"10.1002/cm.21897","url":null,"abstract":"<p>Axonemal dyneins are the driving force of motile cilia, while cytoplasmic dyneins play an essential role in minus-end oriented intracellular transport. Their molecular structure is indispensable for an understanding of the molecular mechanism of ciliary beating and cargo transport. After some initial structural analysis of cytoplasmic dyneins, which are easier to manipulate with genetic engineering, using X-ray crystallography and single-particle cryo-electron microscopy, a number of atomic and pseudo-atomic structural analyses of axonemal dyneins have been published. Currently, several structures of dyneins in the post-power stroke conformation as well as a few structures in the pre-power stroke conformation are available. It will be worth systematically comparing conformations of dynein motor proteins from different sources and at different states, to understand their role in biological function. In this review, we will overview published high- and intermediate-resolution structures of cytoplasmic and axonemal dyneins, compare the high-resolution structures of their core motor domains and overall tail conformations at various nucleotide states, and discuss their force generation mechanism.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 11","pages":"681-690"},"PeriodicalIF":2.4,"publicationDate":"2024-07-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21897","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141774437","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":"Septin complexes: Ahead of the curve","authors":"Mitsutoshi Nakamura, Susan M. Parkhurst","doi":"10.1002/cm.21890","DOIUrl":"https://doi.org/10.1002/cm.21890","url":null,"abstract":"Individual cells have robust repair systems to survive cell cortex damage caused by mechanical and chemical stresses, allowing them to maintain the integrity of tissues and organs. The contraction of an actomyosin ring at the wound edge is a major mechanism for physically closing the cell wound. In contrast to polymerization and bundling of actin filaments, little is known about how linear actin filaments are bent to be integrated into the actin ring structure encircling the wound edge. We recently found that the five <jats:italic>Drosophila</jats:italic> Septins function simultaneously in the regulation of actomyosin ring assembly, contraction, and disassembly during cell wound repair. These Septins form two distinct complexes—Sep1‐Sep2‐Pnut and Sep4‐Sep5‐Pnut—composed of different subunits from the same groups. Strikingly, these two distinct Septin complexes have different degrees of F‐actin bending activities that are consistent with their spatial recruitment: different degrees of curved actin filaments are required for the robust formation of different regions of the actomyosin ring. In addition, we found that the two Septin complexes are regulated by different molecular pathways as a loss of Anillin only affects Sep1‐Sep2‐Pnut complex recruitment. These findings open new directions for how individual Septin subunits form complexes and function differentially in cellular and developmental processes.","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"44 1","pages":""},"PeriodicalIF":2.9,"publicationDate":"2024-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141501554","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":"Structure and function of FAP47 in the central pair apparatus of Chlamydomonas flagella","authors":"Yuma Tani,&nbsp;Haruaki Yanagisawa,&nbsp;Toshiki Yagi,&nbsp;Masahide Kikkawa","doi":"10.1002/cm.21882","DOIUrl":"10.1002/cm.21882","url":null,"abstract":"<p>Motile cilia have a so-called “9 + 2” structure, which consists of nine doublet microtubules and a central pair apparatus. The central pair apparatus (CA) is thought to interact mechanically with radial spokes and to control the flagellar beating. Recently, the components of the CA have been identified by proteomic and genomic analyses. Still, the mechanism of how the CA contributes to ciliary motility has much to be revealed. Here, we focused on one CA component with a large molecular weight: FAP47, and its relationship with two other CA components with large molecular weight: HYDIN, and CPC1. The analyses of motility of the <i>Chlamydomonas</i> mutants revealed that in contrast to <i>cpc1</i> or <i>hydin</i>, which swam more slowly than the wild type, <i>fap47</i> cells displayed wild-type swimming velocity and flagellar beat frequency, yet interestingly, <i>fap47</i> cells have phototaxis defects and swim straighter than the wild-type cells. Furthermore, the double mutant <i>fap47cpc1</i> and <i>fap47hydin</i> showed significantly slower swimming than <i>cpc1</i> and <i>hydin</i> cells, and the motility defect of <i>fap47cpc1</i> was rescued to the <i>cpc1</i> level with GFP-tagged FAP47, indicating that the lack of FAP47 makes the motility defect of <i>cpc1</i> worse. Cryo-electron tomography demonstrated that the <i>fap47</i> lacks a part of the C1–C2 bridge of CA. Taken together, these observations indicate that FAP47 maintains the structural stiffness of the CA, which is important for flagellar regulation.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 11","pages":"669-680"},"PeriodicalIF":2.4,"publicationDate":"2024-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21882","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141428460","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":"Front Cover Image","authors":"","doi":"10.1002/cm.21885","DOIUrl":"https://doi.org/10.1002/cm.21885","url":null,"abstract":"<p>ON THE FRONT COVER: MCF-7 cells treated with compound 2 (published in this issue) and Colchicine and stained with α-tubulin antibody for immunofluorescence (pseudo coloured). Credit: Jianhong Yang (Department of Biotherapy, Cancer Center and State Key Laboratory of Biotherapy. West China Hospital, Sichuan University, Chengdu, China)\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure></p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 6-7","pages":"C1"},"PeriodicalIF":2.9,"publicationDate":"2024-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21885","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141286957","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":"Back Cover Image","authors":"","doi":"10.1002/cm.21886","DOIUrl":"https://doi.org/10.1002/cm.21886","url":null,"abstract":"<p>ON THE BACK COVER: HeLa cells expressing stable EGFP-α-tubulin were treated with 10 εM Cevipabulin for 1 min and monitored for tubulin using confocal fluorescence microscopy. Credit: Jianhong Yang (Department of Biotherapy, Cancer Center and State Key Laboratory of Biotherapy. West China Hospital, Sichuan University, Chengdu, China)\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure></p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 6-7","pages":"C4"},"PeriodicalIF":2.9,"publicationDate":"2024-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21886","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141286944","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 mechanics of cilia and flagella: What we know and what we need to know","authors":"Charles B. Lindemann,&nbsp;Kathleen A. Lesich","doi":"10.1002/cm.21879","DOIUrl":"10.1002/cm.21879","url":null,"abstract":"<p>In this review, we provide a condensed overview of what is currently known about the mechanical functioning of the flagellar/ciliary axoneme. We also present a list of 10 specific areas where our current knowledge is incomplete and explain the benefits of further experimental investigation. Many of the physical parameters of the axoneme and its component parts have not been determined. This limits our ability to understand how the axoneme structure contributes to its functioning in several regards. It restricts our ability to understand how the mechanics of the structure contribute to the regulation of motor function. It also confines our ability to understand the three-dimensional workings of the axoneme and how various beating modes are accomplished. Lastly, it prevents accurate computational modeling of the axoneme in three-dimensions.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 11","pages":"648-668"},"PeriodicalIF":2.4,"publicationDate":"2024-05-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21879","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141082622","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":"Vascular endothelial cell morphology and alignment regulate VEGF-induced endothelial nitric oxide synthase activation","authors":"Aparna Bhattacharyya,&nbsp;Kenneth A. Barbee","doi":"10.1002/cm.21872","DOIUrl":"10.1002/cm.21872","url":null,"abstract":"<p>Nitric oxide (NO) production by endothelial nitric oxide synthase (eNOS) inhibits platelet and leukocyte adhesion while promoting vasorelaxation in smooth muscle cells. Dysfunctional regulation of eNOS is a hallmark of various vascular pathologies, notably atherosclerosis, often associated with areas of low shear stress on endothelial cells (ECs). While the link between EC morphology and local hemodynamics is acknowledged, the specific impact of EC morphology on eNOS regulation remains unclear. Morphological differences between elongated, aligned ECs and polygonal, randomly oriented ECs correspond to variations in focal adhesion and cytoskeletal organization, suggesting differing levels of cytoskeletal prestress. However, the functional outcomes of cytoskeletal prestress, particularly in the absence of shear stress, are not extensively studied in ECs. Some evidence suggests that elongated ECs exhibit decreased immunogenicity and enhanced NO production. This study aims to elucidate the signaling pathways governing VEGF-stimulated eNOS regulation in the aligned EC phenotype characterized by elongated and aligned cells within a monolayer. Using anisotropic topographic cues, bovine aortic endothelial cells (BAECs) were elongated and aligned, followed by VEGF treatment in the presence or absence of cytoskeletal tension inhibitors. Phosphorylation of eNOS ser1179, AKT ser437 and FAK Tyr397 in response to VEGF challenge were significantly heightened in aligned ECs compared to unaligned ECs. Moreover this response proved to be robustly tied to cytoskeletal tension as evinced by the abrogation of responses in the presence of the myosin II ATPase inhibitor, blebbistatin. Notably, this work demonstrates for the first time the reliance on FAK phosphorylation in VEGF-mediated eNOS activation and the comparatively greater contribution of the cytoskeletal machinery in propagating VEGF-eNOS signaling in aligned and elongated ECs. This research underscores the importance of utilizing appropriate vascular models in drug development and sheds light on potential mechanisms underlying vascular function and pathology that can help inform vascular graft design.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 9-10","pages":"473-487"},"PeriodicalIF":2.4,"publicationDate":"2024-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141075693","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}