CytoskeletonPub Date : 2024-12-19DOI: 10.1002/cm.21975
Jagrity Choudhury, Barnali N. Chaudhuri
{"title":"Tubules, Rods, and Spirals: Diverse Modes of SepF-FtsZ Assembling","authors":"Jagrity Choudhury, Barnali N. Chaudhuri","doi":"10.1002/cm.21975","DOIUrl":"10.1002/cm.21975","url":null,"abstract":"<div>\u0000 \u0000 <p>Z-ring formation by FtsZ, the master assembler of the divisome, is a key step in bacterial cell division. Membrane anchoring of the Z-ring requires the assistance of dedicated Z-ring binding proteins, such as SepF and FtsA. SepF participates in bundling and membrane anchoring of FtsZ in gram-positive bacteria. We report in vitro biophysical studies of the interactions between FtsZ and a cytoplasmic component of cognate SepF from three different bacteria: <i>Mycobacterium tuberculosis</i>, <i>Staphylococcus aureus</i>, and <i>Enterococcus gallinarum.</i> While the cytosolic domain of SepF from <i>M. tuberculosis</i> is primarily a dimer, those from <i>S. aureus</i> and <i>E. gallinarum</i> polymerize to form ring-like structures. Mycobacterial SepF helps in the bundling of FtsZ filaments to form thick filaments and large spirals. On the other hand, ring-forming SepF from the <i>Firmicutes</i> bundle FtsZ into tubules. Our results suggest that the oligomeric form of SepF directs how it bundles FtsZ filaments.</p>\u0000 </div>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 7","pages":"432-443"},"PeriodicalIF":2.4,"publicationDate":"2024-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142866740","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 : 2024-12-18DOI: 10.1002/cm.21973
Kyle P. Smith
{"title":"Author Profile: Kyle Paul Smith","authors":"Kyle P. Smith","doi":"10.1002/cm.21973","DOIUrl":"10.1002/cm.21973","url":null,"abstract":"","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 6","pages":"404-405"},"PeriodicalIF":2.4,"publicationDate":"2024-12-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142848156","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 : 2024-12-09DOI: 10.1002/cm.21971
Bat-Ider Tumenbayar, Khanh Pham, John C. Biber, Vincent M. Tutino, Joseph A. Brazzo III, Peng Yao, Yongho Bae
{"title":"FAK and p130Cas Modulate Stiffness-Mediated Early Transcription and Cellular Metabolism","authors":"Bat-Ider Tumenbayar, Khanh Pham, John C. Biber, Vincent M. Tutino, Joseph A. Brazzo III, Peng Yao, Yongho Bae","doi":"10.1002/cm.21971","DOIUrl":"10.1002/cm.21971","url":null,"abstract":"<div>\u0000 \u0000 <p>Cellular metabolism is influenced by the stiffness of the extracellular matrix. Focal adhesion kinase (FAK) and its binding partner, p130Cas, transmit biomechanical signals, such as substrate stiffness, to the cell to regulate a variety of cellular responses, but their roles in early transcriptional and metabolic responses remain largely unexplored. We cultured mouse embryonic fibroblasts with or without siRNA-mediated FAK or p130Cas knockdown and assessed the early transcriptional responses of these cells to placement on soft and stiff substrates by RNA sequencing and bioinformatics analyses. Exposure to the stiff substrate altered the expression of genes important for metabolic and biosynthetic processes, and these responses were influenced by knockdown of FAK and p130Cas. Our findings reveal that FAK-p130Cas signaling mechanotransduces substrate stiffness to early transcriptional changes that alter cellular metabolism and biosynthesis.</p>\u0000 </div>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 3","pages":"197-215"},"PeriodicalIF":2.4,"publicationDate":"2024-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142803724","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 : 2024-12-09DOI: 10.1002/cm.21964
Rosa M. Guerra, Velia M. Fowler, Liyun Wang
{"title":"Osteocyte Dendrites: How Do They Grow, Mature, and Degenerate in Mineralized Bone?","authors":"Rosa M. Guerra, Velia M. Fowler, Liyun Wang","doi":"10.1002/cm.21964","DOIUrl":"10.1002/cm.21964","url":null,"abstract":"<p>Osteocytes, the most abundant bone cells, form an extensive cellular network via interconnecting dendrites. Like neurons in the brain, the long-lived osteocytes perceive mechanical and biological inputs and signal to other effector cells, leading to the homeostasis and turnover of bone tissues. Despite the appreciation of osteocytes' vital roles in bone biology, the initiation, growth, maintenance, and eventual degradation of osteocyte dendrites are poorly understood due to their full encasement by mineralized matrix. With the advancement of imaging modalities and genetic models, the architectural organization and molecular composition of the osteocyte dendrites, as well as their morphological changes with aging and diseases, have begun to be revealed. However, several long-standing mysteries remain unsolved, including (1) how the dendrites are initiated and elongated when a surface osteoblast becomes embedded as an osteocyte; (2) how the dendrites maintain a relatively stable morphology during their decades-long life span; (3) what biological processes control the dendrite morphology, connectivity, and stability; and (4) if these processes are influenced by age, sex, hormones, and mechanical loading. Our review of long, thin actin filament (F-actin)-containing processes extending from other cells leads to a working model that serves as a starting point to investigate the formation and maintenance of osteocyte dendrites and their degradation with aging and diseases.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 9","pages":"556-570"},"PeriodicalIF":1.6,"publicationDate":"2024-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12146430/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142803765","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 : 2024-12-05DOI: 10.1002/cm.21963
Grace Cai, Nicole C. Rodgers, Allen P. Liu
{"title":"Unjamming Transition as a Paradigm for Biomechanical Control of Cancer Metastasis","authors":"Grace Cai, Nicole C. Rodgers, Allen P. Liu","doi":"10.1002/cm.21963","DOIUrl":"10.1002/cm.21963","url":null,"abstract":"<p>Tumor metastasis is a complex phenomenon that poses significant challenges to current cancer therapeutics. While the biochemical signaling involved in promoting motile phenotypes is well understood, the role of biomechanical interactions has recently begun to be incorporated into models of tumor cell migration. Specifically, we propose the unjamming transition, adapted from physical paradigms describing the behavior of granular materials, to better discern the transition toward an invasive phenotype. In this review, we introduce the jamming transition broadly and narrow our discussion to the different modes of 3D tumor cell migration that arise. Then we discuss the mechanical interactions between tumor cells and their neighbors, along with the interactions between tumor cells and the surrounding extracellular matrix. We center our discussion on the interactions that induce a motile state or unjamming transition in these contexts. By considering the interplay between biochemical and biomechanical signaling in tumor cell migration, we can advance our understanding of biomechanical control in cancer metastasis.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 6","pages":"388-403"},"PeriodicalIF":2.4,"publicationDate":"2024-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12137693/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142781931","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 : 2024-12-04DOI: 10.1002/cm.21965
{"title":"Front Cover Image","authors":"","doi":"10.1002/cm.21965","DOIUrl":"https://doi.org/10.1002/cm.21965","url":null,"abstract":"<p>ON THE FRONT COVER: Myosin A staining in the earliest stages of muscle cytoskeletal organization in a comma-stage C. elegans embryos shows an anterior-posterior gradient in the organization of myosin A into a striated pattern.</p><p>Credit: Kar Men Lee and Hao Peng (Western Michigan University Department of Biological Sciences).\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 12","pages":"C1"},"PeriodicalIF":2.4,"publicationDate":"2024-12-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21965","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142762264","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 : 2024-12-04DOI: 10.1002/cm.21966
{"title":"Inner Front Cover Image","authors":"","doi":"10.1002/cm.21966","DOIUrl":"https://doi.org/10.1002/cm.21966","url":null,"abstract":"<p>ON THE INNER FRONT COVER: A genetic mosaic C. elegans adult stained for myosin A and UNC-89 (vertebrate homolog is obscurin) in body-wall muscle shows disorganized UNC-89/obscurin in a muscle cell that does not express myosin A.</p><p>Credit: Sarah Almuhanna (Imam Abdulrahman Bin Faisal University College 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 12","pages":"C2"},"PeriodicalIF":2.4,"publicationDate":"2024-12-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21966","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142762265","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 : 2024-12-04DOI: 10.1002/cm.21968
{"title":"Back Cover Image","authors":"","doi":"10.1002/cm.21968","DOIUrl":"https://doi.org/10.1002/cm.21968","url":null,"abstract":"<p>ON THE BACK COVER: Immunofluorescence analysis of a histological section derived from a cutaneous squamous cell carcinoma specimen. S100A4 (green), primarily expressed by fibroblast cells, cytokeratin 14 (red), primarily expressed by basal epidermal cells, and DAPI (blue) to mark cell nuclei.</p><p>Credit: Alexandra Pittar, Centre for Cancer Biology, an Alliance between SA Pathology and the University of South Australia, Adelaide, Australia.\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 12","pages":"C4"},"PeriodicalIF":2.4,"publicationDate":"2024-12-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21968","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142762263","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}