Group I PAKs function downstream of Rac to promote podosome invasion during myoblast fusion in vivo

Duan, Rui; Jin, Peng; Luo, Fengbao; Zhang, Guofeng; Anderson, Nathan; Chen, Elizabeth H.

doi:10.1083/jcb.201204065

Cited by 43 publications

(64 citation statements)

References 76 publications

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“…S3E-G′). A similar effect on actin distribution has been reported during myoblast fusion in Drosophila embryogenesis when Pak3 function was downregulated (Duan et al, 2012).…”

Section: Pak3 Functions Downstream Of Rac Gtpase In Guidance Receptorsupporting

confidence: 52%

“…Based on our analysis combined with previous findings (Baek et al, 2012;Duan et al, 2012), we propose that Pak3 functions downstream of Rac GTPase in guidance receptor signaling to modulate efficient border cell movement. In Pak3-compromised border cells, the distribution of polarity proteins is significantly altered.…”

Section: Discussionmentioning

confidence: 94%

“…flies (Duan et al, 2012;Baek et al, 2012). Since depletion of Pak3 or guidance receptor function affects the apical-basal polarity of migrating border cells, we proposed that if Rac GTPase functions in the same biochemical pathway as Pak3 then it should also affect the apical-basal polarity of the migrating cluster.…”

Section: Rac1 Mediates Apical-basal Polarity In Moving Border Cellsmentioning

confidence: 99%

“…Since Pak3 protein is expressed in the border cells, we sought to investigate if it has any role in cluster movement. To downregulate Pak3 function effectively in border cells, we overexpressed a dominant-negative construct [Pak3V5(K322A)] in a Pak3 zyg heterozygous mutant background as reported by Duan et al (2012); hereafter, this genetic combination is referred to as Pak3DN. Consistent with our expectation, downregulation of Pak3 function impedes border cell movement in ∼98% of stage 10 egg chambers ( Fig.…”

Section: Pak3 Regulates Border Cell Movementmentioning

confidence: 99%

“…The group I Paks controls various processes, including polarity, whereas Mbt has been linked to cell proliferation and morphogenesis (Asano et al, 2009;Conder et al, 2007;Duan et al, 2012;Melzer et al, 2013;Schneeberger and Raabe, 2003). Our interest was to understand how polarity is regulated in collective cell movement so we focused on the group I Pak and Pak3.…”

Section: Introductionmentioning

confidence: 99%

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dPak3 regulates apical-basal polarity in migrating border cells during Drosophila oogenesis

et al. 2015

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Group cell migration is a highly coordinated process that is involved in a number of physiological events such as morphogenesis, wound healing and tumor metastasis. Unlike single cells, collectively moving cells are physically attached to each other and retain some degree of apical-basal polarity during the migratory phase. Although much is known about direction sensing, how polarity is regulated in multicellular movement remains unclear. Here we report the role of the protein kinase Pak3 in maintaining apical-basal polarity in migrating border cell clusters during Drosophila oogenesis. Pak3 is enriched in border cells and downregulation of its function impedes border cell movement. Time-lapse imaging suggests that Pak3 affects protrusive behavior of the border cell cluster, specifically regulating the stability and directionality of protrusions. Pak3 functions downstream of guidance receptor signaling to regulate the level and distribution of F-actin in migrating border cells. We also provide evidence that Pak3 genetically interacts with the lateral polarity marker Scribble and that it regulates JNK signaling in the moving border cells. Since Pak3 depletion results in mislocalization of several apical-basal polarity markers and overexpression of Jra rescues the polarity of the Pak3-depleted cluster, we propose that Pak3 functions through JNK signaling to modulate apical-basal polarity of the migrating border cell cluster. We also observe loss of apical-basal polarity in Rac1-depleted border cell clusters, suggesting that guidance receptor signaling functions through Rac GTPase and Pak3 to regulate the overall polarity of the cluster and mediate efficient collective movement of the border cells to the oocyte boundary.

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“…S3E-G′). A similar effect on actin distribution has been reported during myoblast fusion in Drosophila embryogenesis when Pak3 function was downregulated (Duan et al, 2012).…”

Section: Pak3 Functions Downstream Of Rac Gtpase In Guidance Receptorsupporting

confidence: 52%

Section: Discussionmentioning

confidence: 94%

Section: Rac1 Mediates Apical-basal Polarity In Moving Border Cellsmentioning

confidence: 99%

Section: Pak3 Regulates Border Cell Movementmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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dPak3 regulates apical-basal polarity in migrating border cells during Drosophila oogenesis

et al. 2015

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Underlying mechanisms that ensure actomyosin‐mediated directional remodeling of cell–cell contacts for multicellular movement

Uechi

Kuranaga

2023

BioEssays

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Actomyosin (actin-myosin II complex)-mediated contractile forces are central to the generation of multifaceted uni-and multi-cellular material properties and dynamics such as cell division, migration, and tissue morphogenesis. In the present article, we summarize our recent researches addressing molecular mechanisms that ensure actomyosin-mediated directional cell-cell junction remodeling, either shortening or extension, driving cell rearrangement for epithelial morphogenesis. Genetic perturbation clarified two points concerning cell-cell junction remodeling: an inhibitory mechanism against negative feedback in which actomyosin contractile forces, which are well known to induce cell-cell junction shortening, can concomitantly alter actin dynamics, oppositely leading to perturbation of the shortening; and tricellular junctions as a point that organizes extension of new cell-cell junctions after shortening.These findings highlight the notion that cells develop underpinning mechanisms to transform the multi-tasking property of actomyosin contractile forces into specific and proper cellular dynamics in space and time.

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A conserved role for calpains during myoblast fusion

Buffolo

Possidonio

Mermelstein

et al. 2015

Genesis

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Myoblast fusion is a key step during skeletal muscle differentiation as it enables the formation of contractile fibers. Calpains have been implicated in some aspects of myogenesis in mammals, but whether they exert a conserved function during myoblast fusion has not been investigated. Here, we studied Calpain function in two models of myogenesis: in vitro analysis of chick myogenic cultures and in vivo analysis of Drosophila melanogaster muscle development. First we showed that Calpain A is important for fly muscle function. In addition, Calpain A knockdown reduced lateral body wall muscle length and width, as well as the number of nuclei in dorsal oblique muscles, consistent with fewer cells fusing to form fibers. Treatment of chick cultures with a selective Calpain inhibitor led to the formation of thinner myotubes containing a reduced number of nuclei, consistent with decreased myoblast fusion. Dynamic changes in IκBα labeling and transfection with a dominant-negative IκBα suggest a role for the NFκB pathway during chick myogenesis and a possible role of Calpains in attenuating NFκB signals that restrict myoblast fusion. Our data suggest that different model organisms may be used to study the role of Calpains in regular myogenesis and Calpain-related muscular degenerative disorders.

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Group I PAKs function downstream of Rac to promote podosome invasion during myoblast fusion in vivo

Abstract: Group I p21-activated kinases organize actin filaments in myoblasts into dense foci, which promote podosome invasion and subsequent myoblast fusion.

Cited by 43 publications

References 76 publications

dPak3 regulates apical-basal polarity in migrating border cells during Drosophila oogenesis

dPak3 regulates apical-basal polarity in migrating border cells during Drosophila oogenesis

Underlying mechanisms that ensure actomyosin‐mediated directional remodeling of cell–cell contacts for multicellular movement

A conserved role for calpains during myoblast fusion

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