Please use this identifier to cite or link to this item: https://doi.org/10.1242/bio.013649
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dc.titleNovel localization of formin mDia2: importin ?-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope
dc.contributor.authorShao, X
dc.contributor.authorKawauchi, K
dc.contributor.authorShivashankar, G.V
dc.contributor.authorBershadsky, A.D
dc.date.accessioned2020-09-14T07:42:03Z
dc.date.available2020-09-14T07:42:03Z
dc.date.issued2015
dc.identifier.citationShao, X, Kawauchi, K, Shivashankar, G.V, Bershadsky, A.D (2015). Novel localization of formin mDia2: importin ?-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope. Biology Open 4 (11) : 1569-1575. ScholarBank@NUS Repository. https://doi.org/10.1242/bio.013649
dc.identifier.issn2046-6390
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/176005
dc.description.abstractThe formin family proteins are important regulators of actin polymerization that are involved in many cellular processes. However, little is known about their specific cellular localizations. Here, we show that Diaphanous-related formin-3 (mDia2) localizes to the cytoplasmic side of the nuclear envelope. This localization of mDia2 to the nuclear rim required the presence of a nuclear localization signal (NLS) sequence at the mDia2 N-terminal. Consistent with this result, super-resolution images demonstrated that at the nuclear rim, mDia2 co-localized with the nuclear pore complexes and a nuclear transport receptor, importin β. Furthermore, an interaction between mDia2 and importin β was detected by immunoprecipitation, and silencing of importin β was shown to attenuate accumulation of mDia2 to the nuclear rim. We have shown previously that Ca2+ entry leads to the assembly of perinuclear actin rim in an inverted formin 2 (INF2) dependent manner. mDia2, however, was not involved in this process since abolishing its localization at the nuclear rim by silencing of importin β had no effect on actin assembly at the nuclear rim triggered by Ca2+ stimulation. © 2015. Published by The Company of Biologists Ltd.
dc.sourceUnpaywall 20200831
dc.subject4 amino 6 [2 [[4 (diethylamino) 1 methylbutyl]amino] 6 methyl 4 pyrimidinyl] 2 methylquinoline
dc.subjectcalcimycin
dc.subjectcalcium ion
dc.subjectdiaphanous related formin 1
dc.subjectdiaphanous related formin 3
dc.subjectF actin
dc.subjectguanosine triphosphatase
dc.subjectinverted formin 2
dc.subjectkaryopherin beta
dc.subjectlamin b1
dc.subjectmethenamine
dc.subjectNup153 protein
dc.subjectprotein
dc.subjectRac1 protein
dc.subjectunclassified drug
dc.subjectactin polymerization
dc.subjectamino terminal sequence
dc.subjectArticle
dc.subjectbioaccumulation
dc.subjectcell function
dc.subjectcell nucleus membrane
dc.subjectcellular distribution
dc.subjectcontrolled study
dc.subjectcytoplasm
dc.subjectfemale
dc.subjectgene silencing
dc.subjecthuman
dc.subjecthuman cell
dc.subjectimmunoprecipitation
dc.subjectnuclear localization signal
dc.subjectnuclear pore complex
dc.subjectprotein interaction
dc.subjectsequence analysis
dc.typeArticle
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.description.doi10.1242/bio.013649
dc.description.sourcetitleBiology Open
dc.description.volume4
dc.description.issue11
dc.description.page1569-1575
dc.published.statePublished
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