Antisocial, an Intracellular Adaptor Protein, Is Required for Myoblast Fusion in Drosophila

Chen, Elizabeth H.; Olson, Eric N.

doi:10.1016/s1534-5807(01)00084-3

Cited by 136 publications

(190 citation statements)

References 33 publications

(2 reference statements)

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“…The insertion site of the EP vector within canB2 was determined by generating a genomic PCR product by using primers from canB2 intron 1 and the EP DNA, followed by cloning of the 258-bp fragment into the TOPO pCRII vector (Invitrogen) and sequencing. canB2 180 ͞CyO-GFP arm (14) was obtained from K. Sullivan (University of California, Berkeley), and MHC-GFP stocks were established as described in Chen and Olson (16). To generate UAS-mcanA act lines, a murine canA␣ cDNA encoding amino acids 1-398 was cloned into the pUAST P element vector.…”

Section: Methodsmentioning

confidence: 99%

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Requirement of the calcineurin subunit gene canB2 for indirect flight muscle formation in Drosophila

Gajewski

Wang

Molkentin

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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Calcineurin is a calcium-activated protein phosphatase involved in multiple aspects of cardiac and skeletal muscle development and disease. Genes encoding calcineurin subunit proteins are highly conserved among animal species. Toward the goal of identifying new calcineurin-interacting loci that function in myogenic processes, we expressed an activated form of mouse calcineurin A in Drosophila and screened for suppressors of the phosphataseinduced lethality. Here, we demonstrate that a mutation in the canB2 gene, which encodes a regulatory subunit of Drosophila calcineurin, can suppress a pupal developmental arrest phenotype to adult viability. As canB2 is an essential gene and rare homozygous escapers are flightless, we further analyzed canB2 expression and function in pupae and adults. The gene is expressed in the forming indirect flight muscles and central nervous system during pupal development. A canA gene is comparably expressed in these tissues. Consistent with the observed muscle expression, canB2 mutants exhibit severe defects in the organization of their indirect flight muscles, a phenotype that is likely caused by muscle hypercontractility. Together, these findings demonstrate a vital role for the phosphatase in this specific facet of Drosophila myogenesis and show conserved fly and vertebrate calcineurin genes contribute prominently to fundamental processes of muscle formation and function.

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Section: Methodsmentioning

confidence: 99%

“…To facilitate phenotypic analyses, EP(2)0774, MHC-GFP was balanced over CyO, GFP-Actin. This combination allows for the easy identification of homozygous EP(2)0774, MHC-GFP larvae because the MHC-GFP transgene expresses strongly in body wall muscles (16), whereas GFP-Actin generates a fluorescent signal in portions of the gut.…”

Section: Methodsmentioning

confidence: 99%

Requirement of the calcineurin subunit gene canB2 for indirect flight muscle formation in Drosophila

Gajewski

Wang

Molkentin

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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“…The cytoplasmatic tails of the adhesion molecules are most likely to be involved in this signal transduction process (Sink, 2006). For example, the intracellular domain of Duf/Kirre is needed to recruit the multidomain protein Rolling Pebbles 7 (Rols7), also known as Antisocial (Ants) (Chen and Olson, 2001;Menon and Chia, 2001). This leads to colocalization of Rols and Duf/Kirre in a ring-like manner within the FuRMAS in the fc/ growing myotube (Kesper et al, 2007).…”

Section: Establishment and Known Components Of The Furmasmentioning

confidence: 99%

“…Immunoprecipitaion (CoIPs) studies with Duf and Rols/Ants or Rols and Mbc after transfection into S2 cells revealed interaction of Rols/Ants with Duf as well as with Mbc (Chen and Olson, 2001). Thus, Rols7/Ants might Fig.…”

Section: Establishment and Known Components Of The Furmasmentioning

confidence: 99%

FuRMAS: triggering myoblast fusion in Drosophila

Önel

Renkawitz‐Pohl

2009

Developmental Dynamics

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In Drosophila, as in mammals, myoblast fusion is fundamental for development. This fusion process has two distinct phases that share common ultrastructural features and at least some molecular players between Drosophila and vertebrates. Here, we integrate the latest data on the key molecular players and ultrastructural features found during myoblast fusion into a new working model to explain this fundamental cellular process. At cell-cell contact sites, a protein complex (

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“…Dumbfounded/Kin-of-IrreC and Roughest/Irregular-optic-chiasma-C are expressed on the founder myoblasts and associate with Stick and Stones and Hibris found at the surface of fusion-competent myoblasts to trigger intracellular signaling cascades leading to fusion (4)(5)(6)(7). The signaling intermediates include scaffold proteins (ELMO, Blown Fuse, Antisocial) (8)(9)(10), kinase (p21-activated kinase) (11), guanine nucleotide exchange factors (GEFs) [Myoblast City (MBC), Loner] (12, 13), GTPase (Rac), (14) and actin nucleation regulators (Kette, WAVE, WASP, WASP-interacting protein) (15)(16)(17)(18)(19). Some of these proteins ultimately promote the formation of actin-driven podosome-like structures in the fusion-competent cells that invade founder cells for membrane fusion (20,21).…”

mentioning

confidence: 99%

G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates

Hamoud

Tran

Croteau

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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113

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Muscle fibers form as a result of myoblast fusion, yet the cell surface receptors regulating this process are unknown in vertebrates. In Drosophila, myoblast fusion involves the activation of the Rac pathway by the guanine nucleotide exchange factor Myoblast City and its scaffolding protein ELMO, downstream of cellsurface cell-adhesion receptors. We previously showed that the mammalian ortholog of Myoblast City, DOCK1, functions in an evolutionarily conserved manner to promote myoblast fusion in mice. In search for regulators of myoblast fusion, we identified the G-protein coupled receptor brain-specific angiogenesis inhibitor (BAI3) as a cell surface protein that interacts with ELMO. In cultured cells, BAI3 or ELMO1/2 loss of function severely impaired myoblast fusion without affecting differentiation and cannot be rescued by reexpression of BAI3 mutants deficient in ELMO binding. The related BAI protein family member, BAI1, is functionally distinct from BAI3, because it cannot rescue the myoblast fusion defects caused by the loss of BAI3 function. Finally, embryonic muscle precursor expression of a BAI3 mutant unable to bind ELMO was sufficient to block myoblast fusion in vivo. Collectively, our findings provide a role for BAI3 in the relay of extracellular fusion signals to their intracellular effectors, identifying it as an essential transmembrane protein for embryonic vertebrate myoblast fusion. myotube formation | myogenesis | model system | ced-12 | RhoGTP

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Antisocial, an Intracellular Adaptor Protein, Is Required for Myoblast Fusion in Drosophila

Cited by 136 publications

References 33 publications

Requirement of the calcineurin subunit gene canB2 for indirect flight muscle formation in Drosophila

Requirement of the calcineurin subunit gene canB2 for indirect flight muscle formation in Drosophila

FuRMAS: triggering myoblast fusion in Drosophila

G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates

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