Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41467-018-07149-2
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dc.titleSyncytial germline architecture is actively maintained by contraction of an internal actomyosin corset
dc.contributor.authorPriti, A
dc.contributor.authorOng, H.T
dc.contributor.authorToyama, Y
dc.contributor.authorPadmanabhan, A
dc.contributor.authorDasgupta, S
dc.contributor.authorKrajnc, M
dc.contributor.authorZaidel-Bar, R
dc.date.accessioned2020-09-04T01:44:32Z
dc.date.available2020-09-04T01:44:32Z
dc.date.issued2018
dc.identifier.citationPriti, A, Ong, H.T, Toyama, Y, Padmanabhan, A, Dasgupta, S, Krajnc, M, Zaidel-Bar, R (2018). Syncytial germline architecture is actively maintained by contraction of an internal actomyosin corset. Nature Communications 9 (1) : 4694. ScholarBank@NUS Repository. https://doi.org/10.1038/s41467-018-07149-2
dc.identifier.issn2041-1723
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/174197
dc.description.abstractSyncytial architecture is an evolutionarily-conserved feature of the germline of many species and plays a crucial role in their fertility. However, the mechanism supporting syncytial organization is largely unknown. Here, we identify a corset-like actomyosin structure within the syncytial germline of Caenorhabditis elegans, surrounding the common rachis. Using laser microsurgery, we demonstrate that actomyosin contractility within this structure generates tension both in the plane of the rachis surface and perpendicular to it, opposing membrane tension. Genetic and pharmacological perturbations, as well as mathematical modeling, reveal a balance of forces within the gonad and show how changing the tension within the actomyosin corset impinges on syncytial germline structure, leading, in extreme cases, to sterility. Thus, our work highlights a unique tissue-level cytoskeletal structure, and explains the critical role of actomyosin contractility in the preservation of a functional germline. © 2018, The Author(s).
dc.publisherNature Publishing Group
dc.sourceUnpaywall 20200831
dc.subjectmyosin adenosine triphosphatase
dc.subjectCaenorhabditis elegans protein
dc.subjectmyosin
dc.subjectmyosin adenosine triphosphatase
dc.subjectamino acid
dc.subjectfertility
dc.subjectgerm cell
dc.subjectlaser
dc.subjectmembrane
dc.subjectnematode
dc.subjectArticle
dc.subjectCaenorhabditis elegans
dc.subjectcytoskeleton
dc.subjectgerm line
dc.subjectgonad
dc.subjectlaser surgery
dc.subjectmathematical model
dc.subjectmicrosurgery
dc.subjectnonhuman
dc.subjectstructure analysis
dc.subjectsurface property
dc.subjecttension
dc.subjectanimal
dc.subjectbiological model
dc.subjectcytoplasmic streaming
dc.subjectgerm cell
dc.subjectgiant cell
dc.subjectmetabolism
dc.subjectCaenorhabditis elegans
dc.subjectActomyosin
dc.subjectAnimals
dc.subjectCaenorhabditis elegans
dc.subjectCaenorhabditis elegans Proteins
dc.subjectCytoplasmic Streaming
dc.subjectGerm Cells
dc.subjectGiant Cells
dc.subjectGonads
dc.subjectModels, Biological
dc.subjectMyosins
dc.typeArticle
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.contributor.departmentDEPT OF BIOMEDICAL ENGINEERING
dc.description.doi10.1038/s41467-018-07149-2
dc.description.sourcetitleNature Communications
dc.description.volume9
dc.description.issue1
dc.description.page4694
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