Redox signaling modulates Rho activity and tissue contractility in the<i>Caenorhabditis elegans</i>spermatheca

Kelley, Charlotte A.; Henau, Sasha De; Bell, Liam; Dansen, Tobias B.; Cram, Erin J.

doi:10.1091/mbc.e20-04-0236

Cited by 6 publications

(8 citation statements)

References 95 publications

(172 reference statements)

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“…In wild type animals, actin and myosin briefly become less colocalized after egg entry into the spermatheca, but become more strongly colocalized during contraction and egg exit ( Figure 2c). This result is consistent across several experiments ( Figure S1), and with previous research demonstrating myosin phosphorylation and activation results in an increase in actomyosin colocalization (Kelley et al, 2018;Kelley, De Henau, Bell, Dansen, & Cram, 2020;Wirshing & Cram, 2017). The fln-1 (tm545) animals exhibit a slow decrease in actomyosin correlation, followed by a precipitate drop as separate foci form (Figure 2b 00 ), and recovery as the tissue relaxes ( Figure 2d).…”

Section: Myosin Forms Perinuclear Foci In Fln-1 Animalssupporting

confidence: 91%

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

et al. 2020

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Actomyosin 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: Myosin Forms Perinuclear Foci In Fln-1 Animalssupporting

confidence: 91%

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

et al. 2020

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“…In wild type animals, actin and myosin briefly become less colocalized after egg entry into the spermatheca, but become more strongly colocalized during contraction and egg exit ( Figure 2C). This result is consistent across several experiments (Supplemental Figure 1), and with previous research demonstrating myosin phosphorylation and activation results in an increase in actomyosin colocalization (Kelley, De Henau, Bell, Dansen, & Cram, 2020;Kelley et al, 2018;Wirshing & Cram, 2017). The fln-1(tm545) animals exhibit a slow decrease in actomyosin correlation, followed by a precipitate drop as separate foci form ( Figure 2B''), and recovery as the tissue relaxes ( Figure 2D).…”

Section: Myosin Forms Perinuclear Foci In Fln-1 Animalssupporting

confidence: 90%

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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“…The spermathecal valves and bag-cells are spatiotemporally coordinated to control oocyte entry during ovulation, as well as oocyte exit after fertilization in the spermatheca. The contractability of the spermathecal tissue is driven by the coordinated activation of myosin ( Kelley and Cram, 2019 ; Kelley et al, 2020a , b ). After ovulation, the fertilized oocytes are expelled from the spermatheca and into the uterus, pushing many sperm with them.…”

Section: Introductionmentioning

confidence: 99%

“…Dysfunctional PEZO-1 resulted in reduced brood size and low ovulation rate, as well as sperm guidance and navigational defects ( Bai et al, 2020a ). Cytoskeletal components play a crucial role in coordinating the contractibility of the spermathecal cells ( Kelley and Cram, 2019 ; Kelley et al, 2020a , b ). Furthermore, PIEZO channels activity is regulated by the cytoskeleton integrity ( Atcha et al, 2021 ; Wang et al, 2022 ; Shmukler et al, 2015 ; Ellefsen et al, 2019 ; Eijkelkamp et al, 2013 ; Pardo-Pastor et al, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

A mutation in F-actin polymerization factor suppresses the distal arthrogryposis type 5 PIEZO2 pathogenic variant in Caenorhabditis elegans

Bai,

Smith,

Romero

et al. 2024

Development

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The mechanosensitive PIEZO channel family has been linked to over 26 disorders and diseases. Although progress has been made in understanding these channels at the structural and functional levels, the underlying mechanisms of PIEZO-associated diseases remain elusive. In this study, we engineered four PIEZO-based disease models using CRISPR/Cas9 gene editing. We performed an unbiased chemical mutagen-based genetic suppressor screen to identify putative suppressors of a conserved gain-of-function variant pezo-1[R2405P] that in human PIEZO2 causes distal arthrogryposis type 5 (DA5; p. R2718P). Electrophysiological analyses indicate that pezo-1(R2405P) is a gain-of-function allele. Using genomic mapping and whole-genome sequencing approaches, we identified a candidate suppressor allele in the C. elegans gene gex-3. This gene is an ortholog of human NCKAP1 (NCK-associated protein 1), a subunit of the Wiskott-Aldrich syndrome protein (WASP)-verprolin homologous protein (WAVE/SCAR) complex, which regulates F-actin polymerization. Depletion of gex-3 by RNAi, or with the suppressor allele gex-3(av259[L353F]), significantly increased brood size and ovulation rate, as well as alleviating the crushed oocyte phenotype of the pezo-1(R2405P) mutant. Expression of GEX-3 in the soma is required to rescue the brood size defects in pezo-1(R2405P) animals. Actin organization and orientation were disrupted and distorted in the pezo-1 mutants. Mutation of gex-3(L353F) partially alleviated these defects. The identification of gex-3 as a suppressor of the pathogenic variant pezo-1(R2405P) suggests that the PIEZO coordinates with the cytoskeleton regulator to maintain the F-actin network and provides insight into the molecular mechanisms of DA5 and other PIEZO-associated diseases.

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Redox signaling modulates Rho activity and tissue contractility in theCaenorhabditis elegansspermatheca

Cited by 6 publications

References 95 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

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

A mutation in F-actin polymerization factor suppresses the distal arthrogryposis type 5 PIEZO2 pathogenic variant in Caenorhabditis elegans

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