Characterisation of the gene for Drosophila amphiphysin

Razzaq, Azam; Ya, SU; Mehren, Jennifer E.; Mizuguchi, Kenji; Jackson, Antony P.; O’Kane, Cahir J.

doi:10.1016/s0378-1119(99)00451-5

Cited by 14 publications

(13 citation statements)

References 30 publications

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“…Moreover, although Drosophila amphiphysin has both an N-terminal BAR domain and C-terminal SH3 domain highly conserved with mammalian amphiphysin 1 and Bin1 isoforms, the central insert domain of mammalian amphiphysin 1 and Bin1ϩ12 that interacts with clathrin heavy chain and AP-2 is not well conserved in Drosophila amphiphysin. Indeed, Drosophila amphiphysin does not bind clathrin heavy chain (169,258,259,386). Hence, Drosophila amphiphysin resembles mammalian Bin1ϩ10ϩ13.…”

Section: Waf1mentioning

confidence: 99%

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

Ren

Vajjhala

Lee

et al. 2006

Microbiol Mol Biol Rev

192

186

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SUMMARY The Bin1/amphiphysin/Rvs167 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt α-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.

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Section: Waf1mentioning

confidence: 99%

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

Ren

Vajjhala

Lee

et al. 2006

Microbiol Mol Biol Rev

192

186

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“…The gene contains 10 exons and occupies ∼17.5 kb of DNA. A homozygous viable P insertion, EP(2)2175, lies 47 bp upstream of the amphiphysin cDNA, LD19810 (Liao et al 2000;Razzaq et al 2000). This insertion was mobilized to generate a number of imprecise excisions; one of these, amph 26 (hereafter referred to as amph mut ), had a deletion of the first exon including the beginning of the coding region, and part of the first intron of the amphiphysin gene (Fig.…”

Section: Generation Of Null Mutations In the Drosophila Amphiphysin Genementioning

confidence: 99%

“…The approximate position of the P insertion in Sin3A 08269 is also shown; the locations of the lesions in the other Sin3A alleles are unknown at this level of resolution. All coordinates are given relative to the first nucleotide of the amphiphysin coding region (Razzaq et al 2000 obvious external defects in eye, bristle, or wing pattern that might result from the interference with endocytic mechanisms involved in wingless, EGF receptor, TGF-␤/decapentaplegic, or Notch signaling (Vieira et al 1996;Seugnet et al 1997;Entchev et al 2000;Dubois et al 2001). Adult mutants were, however, flightless and generally sluggish when homozygous, or when transheterozygous with Df(2R)vg-C. EP(2)2175 homozygotes, amph + homozygotes, and amph + /Df(2R)vg-C heterozygotes all showed no mutant phenotype.…”

Section: Generation Of Null Mutations In the Drosophila Amphiphysin Genementioning

confidence: 99%

Amphiphysin is necessary for organization of the excitation–contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis inDrosophila

Razzaq¹,

Robinson²,

McMahon³

et al. 2001

Genes Dev.

Self Cite

227

257

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Amphiphysins 1 and 2 are enriched in the mammalian brain and are proposed to recruit dynamin to sites of endocytosis. Shorter amphiphysin 2 splice variants are also found ubiquitously, with an enrichment in skeletal muscle. At the Drosophila larval neuromuscular junction, amphiphysin is localized postsynaptically and amphiphysin mutants have no major defects in neurotransmission; they are also viable, but flightless. Like mammalian amphiphysin 2 in muscles, Drosophila amphiphysin does not bind clathrin, but can tubulate lipids and is localized on T-tubules. Amphiphysin mutants have a novel phenotype, a severely disorganized T-tubule/sarcoplasmic reticulum system. We therefore propose that muscle amphiphysin is not involved in clathrin-mediated endocytosis, but in the structural organization of the membrane-bound compartments of the excitation-contraction coupling machinery of muscles.

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“…All BAR gene products include a unique signature domain termed the BAR domain (49), which is evolutionarily conserved among a wide array of eukaryotic organisms (46,47,49). This domain has high ␣-helix-forming potential and can form both homoand heterotypic interactions (20,44,54,62) as well as bind acidic phospholipids (18,56), but it remains functionally illdefined.…”

mentioning

confidence: 99%

Targeted Disruption of the Murine Bin1/Amphiphysin II Gene Does Not Disable Endocytosis but Results in Embryonic Cardiomyopathy with Aberrant Myofibril Formation

Muller

Baker

DuHadaway

et al. 2003

Molecular and Cellular Biology

121

157

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The mammalian Bin1/Amphiphysin II gene encodes an assortment of alternatively spliced adapter proteins that exhibit markedly divergent expression and subcellular localization profiles. Bin1 proteins have been implicated in a variety of different cellular processes, including endocytosis, actin cytoskeletal organization, transcription, and stress responses. To gain insight into the physiological functions of the Bin1 gene, we have disrupted it by homologous recombination in the mouse. Bin1 loss had no discernible impact on either endocytosis or phagocytosis in mouse embryo-derived fibroblasts and macrophages, respectively. Similarly, actin cytoskeletal organization, proliferation, and apoptosis in embryo fibroblasts were all unaffected by Bin1 loss. In vivo, however, Bin1 loss resulted in perinatal lethality. Bin1 has been reported to affect muscle cell differentiation and T-tubule formation. No striking histological abnormalities were evident in skeletal muscle of Bin1 null embryos, but severe ventricular cardiomyopathy was observed in these embryos. Ultrastructurally, myofibrils in ventricular cardiomyocytes of Bin1 null embryos were severely disorganized. These results define a developmentally critical role for the Bin1 gene in cardiac muscle development.

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Characterisation of the gene for Drosophila amphiphysin

Cited by 14 publications

References 30 publications

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

Amphiphysin is necessary for organization of the excitation–contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis inDrosophila

Targeted Disruption of the Murine Bin1/Amphiphysin II Gene Does Not Disable Endocytosis but Results in Embryonic Cardiomyopathy with Aberrant Myofibril Formation

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