Myosin heavy chain-like localizes at cell contact sites during Drosophila myoblast fusion and interacts in vitro with Rolling pebbles 7

Bonn, Bettina R.; Rudolf, Anja; Hornbruch-Freitag, Christina; Daum, Gabor; Kuckwa, Jessica; Kastl, Lena; Buttgereit, Detlev; Renkawitz‐Pohl, Renate

doi:10.1016/j.yexcr.2012.12.005

Cited by 20 publications

(11 citation statements)

References 78 publications

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“…The ability of cells to mix and match multiple NM2 isoforms with multiple M18A isoforms means filaments with a wide range of enzymatic, mechanical, and interaction properties are possible [24][25][26][27]. Importantly, M18 is expressed throughout Metazoa, is widely expressed in vertebrate tissues, and appears to be essential for viability [28] (our unpublished data). Given this and the myriad cellular functions supported by NM2 [29,30], our results have far-reaching functional implications.…”

Section: Discussionmentioning

confidence: 99%

Myosin 18A Coassembles with Nonmuscle Myosin 2 to Form Mixed Bipolar Filaments

et al. 2015

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Nonmusclemyosin 2 (NM-2) powers cell motility and tissue morphogenesis by assembling into bipolar filaments that interact with actin. Although the enzymatic properties of purified NM-2 motor fragments have been determined, the emergent properties of filament ensembles are unknown. Using single myosin filament in vitro motility assays, we report fundamental differences in filaments formed of different NM-2 motors. Filaments consisting of NM2-B moved processively along actin, while under identical conditions, NM2-A filaments did not. By more closely mimicking the physiological milieu, either by increasing solution viscosity or by co-polymerization with NM2-B, NM2-A containing filaments moved processively. Our data demonstrate that both the kinetic and mechanical properties of these two myosins, in addition to the stochiometry of NM-2 subunits, can tune filament mechanical output. We propose altering NM-2 filament composition is a general cellular strategy for tailoring force production of filaments to specific functions, such as maintaining tension or remodeling actin.

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Section: Discussionmentioning

confidence: 99%

Myosin 18A Coassembles with Nonmuscle Myosin 2 to Form Mixed Bipolar Filaments

et al. 2015

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“…Thus, the protrusive and resisting forces from the FCM and the apposing founder cell, respectively, put the fusogenic synapse under high mechanical tension, which helps to overcome energy barriers for membrane apposition and drives cell membrane fusion. Interestingly, another myosin molecule, myosin 18, also accumulates at the fusogenic synapse in the founder cell [48], raising the possibility that the two myosins may function together to modulate cortical tension in founder cells. Future studies are required to investigate the potential functions of Rho, Rok and MyoII in vertebrate myoblast fusion in vivo .…”

Section: The Second Step Toward Myoblast Fusion – Enhancing Cell Membmentioning

confidence: 99%

Mechanisms of myoblast fusion during muscle development

Kim

Jin

Duan

et al. 2015

Current Opinion in Genetics & Development

211

181

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The development and regeneration of skeletal muscles require the fusion of mononulceated muscle cells to form multinucleated, contractile muscle fibers. Studies using a simple genetic model, Drosophila melanogaster, have discovered many evolutionarily conserved fusion-promoting factors in vivo. Recent work in zebrafish and mouse also identified several vertebrate-specific factors required for myoblast fusion. Here, we integrate progress in multiple in vivo systems and highlight conceptual advance in understanding how muscle cell membranes are brought together for fusion. We focus on the molecular machinery at the fusogenic synapse and present a three-step model to describe the molecular and cellular events leading to fusion pore formation.

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“…Specifically, myosin XVIIIB plays a key role in cardiac muscle development and is involved in Drosophila myoblast fusion, and PDZ-containing myosin XVIIIA isoform has been recently found in zebrafish to maintain the stable attachment of myofibers to extracellular matrix and muscle integrity during early development (Ajima et al 2008; Bonn et al 2013; Cao et al 2014). …”

Section: Introductionmentioning

confidence: 99%

Involvement of unconventional myosin VI in myoblast function and myotube formation

Karolczak

Pavlyk

Majewski

et al. 2015

Histochem Cell Biol

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The important role of unconventional myosin VI (MVI) in skeletal and cardiac muscle has been recently postulated (Karolczak et al. in Histochem Cell Biol 139:873–885, 2013). Here, we addressed for the first time a role for this unique myosin motor in myogenic cells as well as during their differentiation into myotubes. During myoblast differentiation, the isoform expression pattern of MVI and its subcellular localization underwent changes. In undifferentiated myoblasts, MVI-stained puncti were seen throughout the cytoplasm and were in close proximity to actin filaments, Golgi apparatus, vinculin-, and talin-rich focal adhesion as well as endoplasmic reticulum. Colocalization of MVI with endoplasmic reticulum was enhanced during myotube formation, and differentiation-dependent association was also seen in sarcoplasmic reticulum of neonatal rat cardiomyocytes (NRCs). Moreover, we observed enrichment of MVI in myotube regions containing acetylcholine receptor-rich clusters, suggesting its involvement in the organization of the muscle postsynaptic machinery. Overexpression of the H246R MVI mutant (associated with hypertrophic cardiomyopathy) in myoblasts and NRCs caused the formation of abnormally large intracellular vesicles. MVI knockdown caused changes in myoblast morphology and inhibition of their migration. On the subcellular level, MVI-depleted myoblasts exhibited aberrations in the organization of actin cytoskeleton and adhesive structures as well as in integrity of Golgi apparatus and endoplasmic reticulum. Also, MVI depletion or overexpression of H246R mutant caused the formation of significantly wider or aberrant myotubes, respectively, indicative of involvement of MVI in myoblast differentiation. The presented results suggest an important role for MVI in myogenic cells and possibly in myoblast differentiation.

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Myosin heavy chain-like localizes at cell contact sites during Drosophila myoblast fusion and interacts in vitro with Rolling pebbles 7

Cited by 20 publications

References 78 publications

Myosin 18A Coassembles with Nonmuscle Myosin 2 to Form Mixed Bipolar Filaments

Myosin 18A Coassembles with Nonmuscle Myosin 2 to Form Mixed Bipolar Filaments

Mechanisms of myoblast fusion during muscle development

Involvement of unconventional myosin VI in myoblast function and myotube formation

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