F-Actin-Dependent Regulation of NESH Dynamics in Rat Hippocampal Neurons

Bae, Jeomil; Sung, Bong Hwan; Cho, In Ha; Song, Woo Keun

doi:10.1371/journal.pone.0034514

Cited by 19 publications

(17 citation statements)

References 30 publications

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“…Smaller fibers have an increased mobile fraction of recovery compared to larger fibers. Altering the stability of actin bundles, either through chemical perturbation, and under-or over-expression of actin binding proteins can change the recovery of actin in FRAP experiments (Bae, Sung, Cho, & Song, 2012;Lorente, Syriani, & Morales, 2014;Pappas, Krieg, & Gregorio, 2010;Zweig & Singer, 1979). In the spermatheca, the mobile fraction of small fibers was around 60%, which is consistent with the mobile fractions of actin recovery seen in the leading edge of lamellipodia in highly motile cancer cells during migration (Lai et al, 2008;Lorente et al, 2014).…”

Section: Discussionsupporting

confidence: 59%

FLN-1/Filamin is required to anchor the actomyosin cytoskeleton and for global organization of sub-cellular organelles in a contractile tissue

Kelley

Triplett

Mallick

et al. 2020

Preprint

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AbstractActomyosin networks are organized in space, direction, size, and connectivity to produce coordinated contractions across cells. We use the C. elegans spermatheca, a tube composed of contractile myoepithelial cells, to study how actomyosin structures are organized. FLN-1/filamin is required for the formation and stabilization of a regular array of parallel, contractile, actomyosin fibers in this tissue. Loss of fln-1 results in the detachment of actin fibers from the basal surface, which then accumulate along the cell junctions and are stabilized by spectrin. In addition, actin and myosin are captured at the nucleus by the linker of nucleoskeleton and cytoskeleton complex (LINC) complex, where they form large foci. Nuclear positioning and morphology, distribution of the endoplasmic reticulum and the mitochondrial network are also disrupted. These results demonstrate that filamin is required to prevent large actin bundle formation and detachment, to prevent excess nuclear localization of actin and myosin, and to ensure correct positioning of organelles.

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Section: Discussionsupporting

confidence: 59%

FLN-1/Filamin is required to anchor the actomyosin cytoskeleton and for global organization of sub-cellular organelles in a contractile tissue

Kelley

Triplett

Mallick

et al. 2020

Preprint

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“…The recovery rate at each time point was determined by dividing the relative intensity of ROI at each time point by the average of the relative intensity of ROI of 3 images taken before photo bleaching. Mobile fraction (MF) was calculated using the equation as follows [13][14][15] : MF D (F end -F post )/(F pre -F post ), where F end is the relative intensity of fluorescence at the endpoint, F post is immediately after photo-bleaching, and F pre is before photo-bleaching.…”

Section: Fluorescence Recovery After Photobleaching (Frap)mentioning

confidence: 99%

Analysis of chromatin structure in mouse preimplantation embryos by fluorescent recovery after photobleaching

et al. 2016

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Zygotes are totipotent cells that have the ability to differentiate into all cell types. It is believed that this ability is lost gradually and differentiation occurs along with the progression of preimplantation development. Here, we hypothesized that the loose chromatin structure is involved in the totipotency of one-cell stage embryos and that the change from loose to tight chromatin structure is associated with the loss of totipotency. To address this hypothesis, we investigated the mobility of eGFP-tagged histone H2B (eGFP-H2B), which is an index for the looseness of chromatin, during preimplantation development based on fluorescent recovery after photobleaching (FRAP) analysis. The highest mobility of eGFP-H2B was observed in pronuclei in 1-cell stage embryos and mobility gradually decreased during preimplantation development. The decrease in mobility between the 1- and 2-cell stages depended on DNA synthesis in 2-cell stage embryos. In nuclear transferred embryos, chromatin in the pseudopronuclei loosened to a level comparable to the pronuclei in 1-cell stage embryos. These results indicated that the mobility of eGFP-H2B is negatively correlated with the degree of differentiation of preimplantation embryos. Therefore, we suggest that highly loosened chromatin is involved in totipotency of 1-cell embryos and the loss of looseness is associated with differentiation during preimplantation development.

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“…Then, Matsuda et al reported that NESH/Abi-3 expression enhanced metastasis in the presence of an Abl inhibitor, imatinib mesylate [ 18 ]. More recently, Bae et al reported that NESH/Abi-3 directly binds to F-actin, and regulates dendritic spine morphogenesis and synapse formation in rat hippocampal neurons [ 19 , 20 ]. These results indicate that NESH/Abi-3 is somehow involved in the regulation of the actin cytoskeleton, but the mechanism remains elusive.…”

Section: Introductionmentioning

confidence: 99%

The NESH/Abi-3-based WAVE2 complex is functionally distinct from the Abi-1-based WAVE2 complex

et al. 2015

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BackgroundAbl interactor (Abi) family proteins play significant roles in actin cytoskeleton organization through participation in the WAVE complex. Mammals possess three Abi proteins: Abi-1, Abi-2, and NESH/Abi-3. Abi-1 and Abi-2 were originally identified as Abl tyrosine kinase-binding proteins. It has been disclosed that Abi-1 acts as a bridge between c-Abl and WAVE2, and c-Abl-mediated WAVE2 phosphorylation promotes actin remodeling. We showed previously that NESH/Abi-3 is present in the WAVE2 complex, but neither binds to c-Abl nor promotes c-Abl-mediated phosphorylation of WAVE2.ResultsIn this study, we characterized NESH/Abi-3 in more detail, and compared its properties with those of Abi-1 and Abi-2. NESH/Abi-3 was ectopically expressed in NIH3T3 cells, in which Abi-1, but not NESH/Abi-3, is expressed. The expression of NESH/Abi-3 caused degradation of endogenous Abi-1, which led to the formation of a NESH/Abi-3-based WAVE2 complex. When these cells were plated on fibronectin-coated dishes, the translocation of WAVE2 to the plasma membrane was significantly reduced and the formation of peripheral lamellipodial structures was disturbed, suggesting that the NESH/Abi-3-based WAVE2 complex was unable to help produce lamellipodial protrusions. Next, Abi-1, Abi-2, or NESH/Abi-3 was expressed in v-src-transformed NIH3T3 cells. Only in NESH/Abi-3-expressed cells did treatment with an Abl kinase inhibitor, imatinib mesylate, or siRNA-mediated knockdown of c-Abl promote the formation of invadopodia, which are ventral membrane protrusions with extracellular matrix degradation activity. Structural studies showed that a linker region between the proline-rich regions and the Src homology 3 (SH3) domain of Abi-1 is crucial for its interaction with c-Abl and c-Abl-mediated phosphorylation of WAVE2.ConclusionsThe NESH/Abi-3-based WAVE2 complex is functionally distinct from the Abi-1-based one, and NESH/Abi-3 may be involved in the formation of ventral protrusions under certain conditions.Electronic supplementary materialThe online version of this article (doi:10.1186/s12964-015-0119-5) contains supplementary material, which is available to authorized users.

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F-Actin-Dependent Regulation of NESH Dynamics in Rat Hippocampal Neurons

Cited by 19 publications

References 30 publications

FLN-1/Filamin is required to anchor the actomyosin cytoskeleton and for global organization of sub-cellular organelles in a contractile tissue

FLN-1/Filamin is required to anchor the actomyosin cytoskeleton and for global organization of sub-cellular organelles in a contractile tissue

Analysis of chromatin structure in mouse preimplantation embryos by fluorescent recovery after photobleaching

The NESH/Abi-3-based WAVE2 complex is functionally distinct from the Abi-1-based WAVE2 complex

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