2011
DOI: 10.1002/dneu.20923
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Barfly: Sculpting membranes at the Drosophila neuromuscular junction

Abstract: The ability of a cell to change the shape of its membranes is intrinsic to many cellular functions. Proteins that can alter or recognize curved membrane structures and those that can act to recruit other proteins which stabilize the membrane curvature are likely to be essential in cell functions. The BAR (Bin, amphiphysin, RVS167 homology) domain is a protein domain that can either induce lipidic membranes to curve or can sense curved membranes. BAR domains are found in several proteins at neuronal synapses. W… Show more

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Cited by 5 publications
(6 citation statements)
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“…In wild‐type larval NMJs, a branching parent bouton normally has no more than two new branches . Mutants that exhibit the satellite bouton phenotype have parent boutons with 3–5 small boutons budding from the parent bouton (Figure (e) and (f)). Satellite boutons are also seen budding off from the axonal segment that connects two adjacent boutons .…”
Section: Nmj Developmentmentioning
confidence: 99%
“…In wild‐type larval NMJs, a branching parent bouton normally has no more than two new branches . Mutants that exhibit the satellite bouton phenotype have parent boutons with 3–5 small boutons budding from the parent bouton (Figure (e) and (f)). Satellite boutons are also seen budding off from the axonal segment that connects two adjacent boutons .…”
Section: Nmj Developmentmentioning
confidence: 99%
“…This mechanism depends on Wit and Sax/Tkv, but not on transcription and is inhibited by Dlp (Glypican) tubular-lamellar membrane folds that envelops the presynaptic bouton [214][215][216][217] that has been described as the structural and functional equivalent of dendritic spines at the Drosophila NMJ [218]. Another notable regulator of SSR expansion is Syndapin (Synd), a member of the F-BAR family of membrane-sculpting proteins [219,220] that appears to exclusively postsynaptic where it likely mediates SSR development by regulating the muscle actin cytoskeleton [221,222]. Development of the SSR also requires additional actinregulatory proteins concentrated in the postsynaptic cytomatrix, including hu-li tai shao (Hts)/Adducin, an actin-capping protein [223][224][225], and Enabled (Ena) [226], which promotes the assembly of linear F-actin; other key cytoskeletal regulators of SSR morphogenesis include both pre-and postsynaptic Spectrin [227,228] and presynaptic Ankyrin [229,230].…”
Section: The Postsynaptic Cytomatrixmentioning
confidence: 99%
“…The orchestration of these biological phenomena hinges on the dynamic interplay between membrane dynamics and the underlying cytoskeleton, primarily composed of actin and microtubule networks (Mallik and Kumar, 2018; Safari and Suetsugu, 2012; Stanishneva-Konovalova et al, 2016). Several proteins, including Bin/Amphiphysin/Rvs161/167 (BAR) domain proteins, are recognized as critical modulators for inducing membrane dynamics (Mallik et al, 2022; Oh and Robinson, 2012; Richnau et al, 2004). The BAR domain, known to form functional dimers, binds to negatively charged membranes, generating curvature crucial for various cellular events (Peter et al, 2004).…”
Section: Introductionmentioning
confidence: 99%