Please use this identifier to cite or link to this item: https://doi.org/10.7554/eLife.33555
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dc.titleVibrator and PI4KIII? govern neuroblast polarity by anchoring non-muscle myosin II
dc.contributor.authorKoe C.T.
dc.contributor.authorTan Y.S.
dc.contributor.authorLönnfors M.
dc.contributor.authorHur S.K.
dc.contributor.authorLow C.S.L.
dc.contributor.authorZhang Y.
dc.contributor.authorKanchanawong P.
dc.contributor.authorBankaitis V.A.
dc.contributor.authorWang H.
dc.date.accessioned2020-09-09T03:12:09Z
dc.date.available2020-09-09T03:12:09Z
dc.date.issued2018
dc.identifier.citationKoe C.T., Tan Y.S., Lönnfors M., Hur S.K., Low C.S.L., Zhang Y., Kanchanawong P., Bankaitis V.A., Wang H. (2018). Vibrator and PI4KIII? govern neuroblast polarity by anchoring non-muscle myosin II. eLife 7 : e33555. ScholarBank@NUS Repository. https://doi.org/10.7554/eLife.33555
dc.identifier.issn2050084X
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/175067
dc.description.abstractA central feature of most stem cells is the ability to self-renew and undergo differentiation via asymmetric division. However, during asymmetric division the role of phosphatidylinositol (PI) lipids and their regulators is not well established. Here, we show that the sole type I PI transfer protein, Vibrator, controls asymmetric division of Drosophilaneural stem cells (NSCs) by physically anchoring myosin II regulatory light chain, Sqh, to the NSC cortex. Depletion of vib or disruption of its lipid binding and transfer activities disrupts NSC polarity. We propose that Vib stimulates PI4KIIIa to promote synthesis of a plasma membrane pool of phosphatidylinositol 4-phosphate [PI(4)P] that, in turn, binds and anchors myosin to the NSC cortex. Remarkably, Sqh also binds to PI(4)P in vitro and both Vib and Sqh mediate plasma membrane localization of PI(4)P in NSCs. Thus, reciprocal regulation between Myosin and PI(4)P likely governs asymmetric division of NSCs. © Koe et al.
dc.sourceUnpaywall 20200831
dc.subjectarsenosobenzene
dc.subjectcarrier protein
dc.subjectlipid binding protein
dc.subjectmyosin II
dc.subjectphosphatidylinositol 4 phosphate
dc.subjectphosphatidylinositol kinase
dc.subjectDrosophila protein
dc.subjectminor histocompatibility antigen
dc.subjectmyosin II
dc.subjectphosphatidylinositol phosphate 4-kinase
dc.subjectphospholipid transfer protein
dc.subjectphosphotransferase
dc.subjectprotein binding
dc.subjectSqh protein, Drosophila
dc.subjectVib protein, Drosophila
dc.subjectanimal cell
dc.subjectArticle
dc.subjectbinding assay
dc.subjectbrain asymmetry
dc.subjectcell division
dc.subjectcell membrane
dc.subjectcell polarity
dc.subjectclone
dc.subjecthomeostasis
dc.subjectimmunoblotting
dc.subjectimmunohistochemistry
dc.subjectin vivo study
dc.subjectlight chain
dc.subjectmitosis spindle
dc.subjectmolecular cloning
dc.subjectneuroblast
dc.subjectnonhuman
dc.subjectnucleolus
dc.subjectprotein lipid interaction
dc.subjectsequence alignment
dc.subjectstem cell
dc.subjecttransgenic fish
dc.subjectanimal
dc.subjectbrain
dc.subjectDrosophila
dc.subjectgrowth, development and aging
dc.subjectlarva
dc.subjectmetabolism
dc.subjectneural stem cell
dc.subjectphysiology
dc.subjectAnimals
dc.subjectBrain
dc.subjectCell Polarity
dc.subjectDrosophila
dc.subjectDrosophila Proteins
dc.subjectLarva
dc.subjectMinor Histocompatibility Antigens
dc.subjectMyosin Type II
dc.subjectNeural Stem Cells
dc.subjectPhospholipid Transfer Proteins
dc.subjectPhosphotransferases (Alcohol Group Acceptor)
dc.subjectProtein Binding
dc.typeArticle
dc.contributor.departmentDUKE-NUS MEDICAL SCHOOL
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.contributor.departmentBIOMEDICAL ENGINEERING
dc.description.doi10.7554/eLife.33555
dc.description.sourcetitleeLife
dc.description.volume7
dc.description.pagee33555
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