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This protein seems to make a link between TDP-43 malfunction, axonal transport problems and loss of neuromuscular junctions in drosophila.

 

  1. Simon Lepicard, Bénédicte Franco, Frédéric Bock and Marie-Laure Parmentier.
    A presynaptic role of microtubule-associated protein 1/Futsch in Drosophila: regulation of active zone number and neurotransmitter release.. The Journal of neuroscience : the official journal of the Society for Neuroscience 34(20):6759–71, May 2014.
    Abstract Structural microtubule-associated proteins (MAPs), like MAP1, not only control the stability of microtubules, but also interact with postsynaptic proteins in the nervous system. Their presynaptic role has barely been studied. To tackle this question, we used the Drosophila model in which there is only one MAP1 homolog: Futsch, which is expressed at the larval neuromuscular junction, presynaptically only. We show that Futsch regulates neurotransmitter release and active zone density. Importantly, we provide evidence that this role of Futsch is not just the consequence of its microtubule-stabilizing function. Using high-resolution microscopy, we show that Futsch and microtubules are almost systematically present in close proximity to active zones, with Futsch being localized in-between microtubules and active zones. Using proximity ligation assays, we further demonstrate the proximity of Futsch, but not microtubules, to active zone components. Altogether our data are in favor of a model by which Futsch locally stabilizes active zones, by reinforcing their link with the underlying microtubule cytoskeleton.
    URL, DOI BibTeX

    @article{Lepicard2014,
    	abstract = "Structural microtubule-associated proteins (MAPs), like MAP1, not only control the stability of microtubules, but also interact with postsynaptic proteins in the nervous system. Their presynaptic role has barely been studied. To tackle this question, we used the Drosophila model in which there is only one MAP1 homolog: Futsch, which is expressed at the larval neuromuscular junction, presynaptically only. We show that Futsch regulates neurotransmitter release and active zone density. Importantly, we provide evidence that this role of Futsch is not just the consequence of its microtubule-stabilizing function. Using high-resolution microscopy, we show that Futsch and microtubules are almost systematically present in close proximity to active zones, with Futsch being localized in-between microtubules and active zones. Using proximity ligation assays, we further demonstrate the proximity of Futsch, but not microtubules, to active zone components. Altogether our data are in favor of a model by which Futsch locally stabilizes active zones, by reinforcing their link with the underlying microtubule cytoskeleton.",
    	author = "Lepicard, Simon and Franco, B\'{e}n\'{e}dicte and de Bock, Fr\'{e}d\'{e}ric and Parmentier, Marie-Laure",
    	doi = "10.1523/JNEUROSCI.4282-13.2014",
    	issn = "1529-2401",
    	journal = "The Journal of neuroscience : the official journal of the Society for Neuroscience",
    	keywords = "Animals,Animals, Genetically Modified,Axonal Transport,Axonal Transport: genetics,Cytoskeleton,Cytoskeleton: genetics,Cytoskeleton: metabolism,Drosophila,Drosophila Proteins,Drosophila Proteins: genetics,Drosophila Proteins: metabolism,Glutamic Acid,Glutamic Acid: metabolism,Microtubule-Associated Proteins,Microtubule-Associated Proteins: genetics,Microtubule-Associated Proteins: metabolism,Microtubules,Microtubules: genetics,Microtubules: metabolism,Neuromuscular Junction,Neuromuscular Junction: genetics,Neuromuscular Junction: metabolism,Presynaptic Terminals,Presynaptic Terminals: metabolism,Synaptic Transmission,Synaptic Transmission: physiology",
    	month = "may",
    	number = 20,
    	pages = "6759--71",
    	pmid = 24828631,
    	title = "{A presynaptic role of microtubule-associated protein 1/Futsch in Drosophila: regulation of active zone number and neurotransmitter release.}",
    	url = "http://www.ncbi.nlm.nih.gov/pubmed/24828631",
    	volume = 34,
    	year = 2014
    }
    
  2. Vinay K Godena, Giulia Romano, Maurizio Romano, Chiara Appocher, Raffaella Klima, Emanuele Buratti, Francisco E Baralle and Fabian Feiguin.
    TDP-43 regulates Drosophila neuromuscular junctions growth by modulating Futsch/MAP1B levels and synaptic microtubules organization.. PloS one 6(3):e17808, 2011.
    Abstract TDP-43 is an evolutionarily conserved RNA binding protein recently associated with the pathogenesis of different neurological diseases. At the moment, neither its physiological role in vivo nor the mechanisms that may lead to neurodegeneration are well known. Previously, we have shown that TDP-43 mutant flies presented locomotive alterations and structural defects at the neuromuscular junctions. We have now investigated the functional mechanism leading to these phenotypes by screening several factors known to be important for synaptic growth or bouton formation. As a result we found that alterations in the organization of synaptic microtubules correlate with reduced protein levels in the microtubule associated protein futsch/MAP1B. Moreover, we observed that TDP-43 physically interacts with futsch mRNA and that its RNA binding capacity is required to prevent futsch down regulation and synaptic defects.
    URL, DOI BibTeX

    @article{Godena2011,
    	abstract = "TDP-43 is an evolutionarily conserved RNA binding protein recently associated with the pathogenesis of different neurological diseases. At the moment, neither its physiological role in vivo nor the mechanisms that may lead to neurodegeneration are well known. Previously, we have shown that TDP-43 mutant flies presented locomotive alterations and structural defects at the neuromuscular junctions. We have now investigated the functional mechanism leading to these phenotypes by screening several factors known to be important for synaptic growth or bouton formation. As a result we found that alterations in the organization of synaptic microtubules correlate with reduced protein levels in the microtubule associated protein futsch/MAP1B. Moreover, we observed that TDP-43 physically interacts with futsch mRNA and that its RNA binding capacity is required to prevent futsch down regulation and synaptic defects.",
    	author = "Godena, Vinay K and Romano, Giulia and Romano, Maurizio and Appocher, Chiara and Klima, Raffaella and Buratti, Emanuele and Baralle, Francisco E and Feiguin, Fabian",
    	doi = "10.1371/journal.pone.0017808",
    	file = ":C$\backslash$:/Users/riku/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Godena et al. - 2011 - TDP-43 regulates Drosophila neuromuscular junctions growth by modulating FutschMAP1B levels and synaptic microtub.pdf:pdf",
    	issn = "1932-6203",
    	journal = "PloS one",
    	keywords = "Acetylation,Animals,DNA-Binding Proteins,DNA-Binding Proteins: metabolism,Drosophila Proteins,Drosophila Proteins: genetics,Drosophila Proteins: metabolism,Drosophila melanogaster,Drosophila melanogaster: metabolism,Microtubule-Associated Proteins,Microtubule-Associated Proteins: genetics,Microtubule-Associated Proteins: metabolism,Microtubules,Microtubules: metabolism,Mutation,Mutation: genetics,Neuromuscular Junction,Neuromuscular Junction: growth \& development,Neuromuscular Junction: metabolism,Presynaptic Terminals,Presynaptic Terminals: metabolism,Protein Binding,RNA, Messenger,RNA, Messenger: genetics,RNA, Messenger: metabolism,Synapses,Synapses: metabolism,Tubulin,Tubulin: metabolism",
    	month = "",
    	number = 3,
    	pages = "e17808",
    	pmid = 21412434,
    	title = "{TDP-43 regulates Drosophila neuromuscular junctions growth by modulating Futsch/MAP1B levels and synaptic microtubules organization.}",
    	url = "http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3055892\&tool=pmcentrez\&rendertype=abstract",
    	volume = 6,
    	year = 2011
    }
    
  3. Seongsoo Lee, Hsin-Ping Liu, Wei-Yong Lin, Huifu Guo and Bingwei Lu.
    LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsynaptic compartments of the Drosophila neuromuscular junction.. The Journal of neuroscience : the official journal of the Society for Neuroscience 30(50):16959–69, 2010.
    Abstract Mutations in leucine-rich repeat kinase 2 (LRRK2) are linked to familial as well as sporadic forms of Parkinson's disease (PD), a neurodegenerative disease characterized by dysfunction and degeneration of dopaminergic and other types of neurons. The molecular and cellular mechanisms underlying LRRK2 action remain poorly defined. Here, we show that LRRK2 controls synaptic morphogenesis at the Drosophila neuromuscular junction. Loss of Drosophila LRRK2 results in synaptic overgrowth, whereas overexpression of Drosophila LRRK or human LRRK2 has opposite effects. Alteration of LRRK2 activity also affects neurotransmission. LRRK2 exerts its effects on synaptic morphology by interacting with distinct downstream effectors at the presynaptic and postsynaptic compartments. At the postsynapse, LRRK2 interacts with the previously characterized substrate 4E-BP, an inhibitor of protein synthesis. At the presynapse, LRRK2 phosphorylates and negatively regulates the microtubule (MT)-binding protein Futsch. These results implicate synaptic dysfunction caused by deregulated protein synthesis and aberrant MT dynamics in LRRK2 pathogenesis and offer a new paradigm for understanding and ultimately treating PD.
    URL, DOI BibTeX

    @article{Lee2010,
    	abstract = "Mutations in leucine-rich repeat kinase 2 (LRRK2) are linked to familial as well as sporadic forms of Parkinson's disease (PD), a neurodegenerative disease characterized by dysfunction and degeneration of dopaminergic and other types of neurons. The molecular and cellular mechanisms underlying LRRK2 action remain poorly defined. Here, we show that LRRK2 controls synaptic morphogenesis at the Drosophila neuromuscular junction. Loss of Drosophila LRRK2 results in synaptic overgrowth, whereas overexpression of Drosophila LRRK or human LRRK2 has opposite effects. Alteration of LRRK2 activity also affects neurotransmission. LRRK2 exerts its effects on synaptic morphology by interacting with distinct downstream effectors at the presynaptic and postsynaptic compartments. At the postsynapse, LRRK2 interacts with the previously characterized substrate 4E-BP, an inhibitor of protein synthesis. At the presynapse, LRRK2 phosphorylates and negatively regulates the microtubule (MT)-binding protein Futsch. These results implicate synaptic dysfunction caused by deregulated protein synthesis and aberrant MT dynamics in LRRK2 pathogenesis and offer a new paradigm for understanding and ultimately treating PD.",
    	author = "Lee, Seongsoo and Liu, Hsin-Ping and Lin, Wei-Yong and Guo, Huifu and Lu, Bingwei",
    	doi = "10.1523/JNEUROSCI.1807-10.2010",
    	file = ":C$\backslash$:/Users/riku/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Lee et al. - 2010 - LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsynaptic compartme.pdf:pdf",
    	issn = "1529-2401",
    	journal = "The Journal of neuroscience : the official journal of the Society for Neuroscience",
    	keywords = "Animals,Drosophila,Drosophila Proteins,Drosophila Proteins: genetics,Drosophila Proteins: metabolism,Drosophila Proteins: physiology,Drosophila: growth \& development,Gene Expression Regulation,Gene Expression Regulation: genetics,Humans,Intracellular Signaling Peptides and Proteins,Intracellular Signaling Peptides and Proteins: met,Microtubule-Associated Proteins,Microtubule-Associated Proteins: metabolism,Miniature Postsynaptic Potentials,Miniature Postsynaptic Potentials: physiology,Morphogenesis,Morphogenesis: genetics,Mutation,Neuromuscular Junction,Neuromuscular Junction: cytology,Neuromuscular Junction: physiology,Peptide Initiation Factors,Peptide Initiation Factors: metabolism,Protein-Serine-Threonine Kinases,Protein-Serine-Threonine Kinases: genetics,Protein-Serine-Threonine Kinases: metabolism,Protein-Serine-Threonine Kinases: physiology,Synapses,Synapses: metabolism,Synapses: physiology",
    	month = "",
    	number = 50,
    	pages = "16959--69",
    	pmid = 21159966,
    	title = "{LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsynaptic compartments of the Drosophila neuromuscular junction.}",
    	url = "http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3045823\&tool=pmcentrez\&rendertype=abstract",
    	volume = 30,
    	year = 2010
    }
    
  4. J E Ellis, L Parker, J Cho and K Arora.
    Activin signaling functions upstream of Gbb to regulate synaptic growth at the Drosophila neuromuscular junction.. Developmental biology 342(2):121–33, 2010.
    Abstract Activins are members of the TGF-ss superfamily of secreted growth factors that control a diverse array of processes in vertebrates including endocrine function, cell proliferation, differentiation, immune response and wound repair. In Drosophila, the Activin ligand Dawdle (Daw) has been shown to regulate several aspects of neuronal development such as embryonic axonal pathfinding, neuroblast proliferation in the larval brain and growth cone motility in the visual system. Here we identify a novel role for Activin signaling in regulating synaptic growth at the larval neuromuscular junction (NMJ). Mutants for Daw, the Activin type I receptor Baboon (Babo), and the signal transducer dSmad2, display reduced NMJ size suggesting that Daw utilizes a canonical Activin signal-transduction pathway in this context. Additionally, loss of Daw/Babo activity affects microtubule stability, axonal transport and distribution of Futsch, the Drosophila microtubule associated protein 1B (MAP1B) homolog. We find that Babo signaling is required postsynaptically in the muscle, in contrast to the well-characterized retrograde BMP/Gbb signal that is required for synaptic growth and function in presynaptic cells. Finally, we show that the Daw/Babo pathway acts upstream of gbb, and is involved in maintenance of muscle gbb expression, suggesting that Activins regulate NMJ growth by modulating BMP activity through transcriptional regulation of ligand expression.
    URL, DOI BibTeX

    @article{Ellis2010,
    	abstract = "Activins are members of the TGF-ss superfamily of secreted growth factors that control a diverse array of processes in vertebrates including endocrine function, cell proliferation, differentiation, immune response and wound repair. In Drosophila, the Activin ligand Dawdle (Daw) has been shown to regulate several aspects of neuronal development such as embryonic axonal pathfinding, neuroblast proliferation in the larval brain and growth cone motility in the visual system. Here we identify a novel role for Activin signaling in regulating synaptic growth at the larval neuromuscular junction (NMJ). Mutants for Daw, the Activin type I receptor Baboon (Babo), and the signal transducer dSmad2, display reduced NMJ size suggesting that Daw utilizes a canonical Activin signal-transduction pathway in this context. Additionally, loss of Daw/Babo activity affects microtubule stability, axonal transport and distribution of Futsch, the Drosophila microtubule associated protein 1B (MAP1B) homolog. We find that Babo signaling is required postsynaptically in the muscle, in contrast to the well-characterized retrograde BMP/Gbb signal that is required for synaptic growth and function in presynaptic cells. Finally, we show that the Daw/Babo pathway acts upstream of gbb, and is involved in maintenance of muscle gbb expression, suggesting that Activins regulate NMJ growth by modulating BMP activity through transcriptional regulation of ligand expression.",
    	author = "Ellis, J E and Parker, L and Cho, J and Arora, K",
    	doi = "10.1016/j.ydbio.2010.03.012",
    	issn = "1095-564X",
    	journal = "Developmental biology",
    	keywords = "Activin Receptors,Activin Receptors: metabolism,Activins,Activins: metabolism,Animals,Carrier Proteins,Carrier Proteins: metabolism,Drosophila Proteins,Drosophila Proteins: metabolism,Drosophila melanogaster,Drosophila melanogaster: metabolism,Neuromuscular Junction,Neuromuscular Junction: metabolism,Transforming Growth Factor beta,Transforming Growth Factor beta: metabolism",
    	month = "",
    	number = 2,
    	pages = "121--33",
    	pmid = 20346940,
    	title = "{Activin signaling functions upstream of Gbb to regulate synaptic growth at the Drosophila neuromuscular junction.}",
    	url = "http://www.ncbi.nlm.nih.gov/pubmed/20346940",
    	volume = 342,
    	year = 2010
    }
    
  5. Shuang Chang, Steven M Bray, Zigang Li, Daniela C Zarnescu, Chuan He, Peng Jin and Stephen T Warren.
    Identification of small molecules rescuing fragile X syndrome phenotypes in Drosophila.. Nature chemical biology 4(4):256–63, 2008.
    Abstract Fragile X syndrome is caused by the functional loss of the fragile X mental retardation 1 (FMR1) gene. Deletion of the FMR1 ortholog in Drosophila melanogaster (Fmr1) recapitulates many phenotypes associated with fragile X syndrome. We have discovered that Fmr1 mutant Drosophila die during development when reared on food containing increased levels of glutamate, which is consistent with the theory that FMR1 loss results in excess glutamate signaling. Using this lethal phenotype, we screened a chemical library of 2,000 compounds and identified nine molecules that rescued the lethality, including three that implicate the GABAergic inhibitory pathway. Indeed, GABA treatment rescued several known Fmr1 mutant phenotypes in flies, including mushroom bodies defects, excess Futsch translation and abnormal male courtship behavior. These data are consistent with GABAergic inhibition of the enhanced excitatory pathway in fragile X syndrome. In addition, our screen reveals that the muscarinic cholinergic receptors may have a role in fragile X syndrome in parallel to the GABAergic pathway. These results point to potential therapeutic approaches for treating fragile X syndrome.
    URL, DOI BibTeX

    @article{Chang2008,
    	abstract = "Fragile X syndrome is caused by the functional loss of the fragile X mental retardation 1 (FMR1) gene. Deletion of the FMR1 ortholog in Drosophila melanogaster (Fmr1) recapitulates many phenotypes associated with fragile X syndrome. We have discovered that Fmr1 mutant Drosophila die during development when reared on food containing increased levels of glutamate, which is consistent with the theory that FMR1 loss results in excess glutamate signaling. Using this lethal phenotype, we screened a chemical library of 2,000 compounds and identified nine molecules that rescued the lethality, including three that implicate the GABAergic inhibitory pathway. Indeed, GABA treatment rescued several known Fmr1 mutant phenotypes in flies, including mushroom bodies defects, excess Futsch translation and abnormal male courtship behavior. These data are consistent with GABAergic inhibition of the enhanced excitatory pathway in fragile X syndrome. In addition, our screen reveals that the muscarinic cholinergic receptors may have a role in fragile X syndrome in parallel to the GABAergic pathway. These results point to potential therapeutic approaches for treating fragile X syndrome.",
    	author = "Chang, Shuang and Bray, Steven M and Li, Zigang and Zarnescu, Daniela C and He, Chuan and Jin, Peng and Warren, Stephen T",
    	doi = "10.1038/nchembio.78",
    	issn = "1552-4469",
    	journal = "Nature chemical biology",
    	keywords = "Animals,Disease Models, Animal,Drosophila,Drosophila Proteins,Drosophila Proteins: drug effects,Drosophila Proteins: genetics,Drosophila: genetics,Drug Evaluation, Preclinical,Drug Evaluation, Preclinical: methods,Female,Fragile X Mental Retardation Protein,Fragile X Mental Retardation Protein: drug effects,Fragile X Mental Retardation Protein: genetics,Fragile X Syndrome,Fragile X Syndrome: genetics,Glutamic Acid,Glutamic Acid: pharmacology,Male,Molecular Weight,Mutation,Phenotype,Pyridines,Pyridines: pharmacology,RNA, Messenger,RNA, Messenger: drug effects,RNA, Messenger: genetics,Small Molecule Libraries,Small Molecule Libraries: chemical synthesis,Small Molecule Libraries: chemistry,gamma-Aminobutyric Acid,gamma-Aminobutyric Acid: drug effects,gamma-Aminobutyric Acid: metabolism,gamma-Aminobutyric Acid: pharmacology",
    	month = "",
    	number = 4,
    	pages = "256--63",
    	pmid = 18327252,
    	title = "{Identification of small molecules rescuing fragile X syndrome phenotypes in Drosophila.}",
    	url = "http://www.ncbi.nlm.nih.gov/pubmed/18327252",
    	volume = 4,
    	year = 2008
    }
    
  6. Alexandre Bettencourt da Cruz, Martin Schwärzel, Sabine Schulze, Mahtab Niyyati, Martin Heisenberg and Doris Kretzschmar.
    Disruption of the MAP1B-related protein FUTSCH leads to changes in the neuronal cytoskeleton, axonal transport defects, and progressive neurodegeneration in Drosophila.. Molecular biology of the cell 16(5):2433–42, 2005.
    Abstract The elaboration of neuronal axons and dendrites is dependent on a functional cytoskeleton. Cytoskeletal components have been shown to play a major role in the maintenance of the nervous system through adulthood, and changes in neurofilaments and microtubule-associated proteins (MAPs) have been linked to a variety of neurodegenerative diseases. Here we show that Futsch, the fly homolog of MAP1B, is involved in progressive neurodegeneration. Although Futsch is widely expressed throughout the CNS, degeneration in futsch(olk) primarily occurs in the olfactory system and mushroom bodies. Consistent with the predicted function of Futsch, we find abnormalities in the microtubule network and defects in axonal transport. Degeneration in the adult brain is preceded by learning deficits, revealing a neuronal dysfunction before detectable levels of cell death. Futsch is negatively regulated by the Drosophila Fragile X mental retardation gene, and a mutation in this gene delays the onset of neurodegeneration in futsch(olk). A similar effect is obtained by expression of either fly or bovine tau, suggesting a certain degree of functional redundancy of MAPs. The futsch(olk) mutants exhibit several characteristics of human neurodegenerative diseases, providing an opportunity to study the role of MAPs in progressive neurodegeneration within an experimentally accessible, in vivo model system.
    URL, DOI BibTeX

    @article{BettencourtdaCruz2005,
    	abstract = "The elaboration of neuronal axons and dendrites is dependent on a functional cytoskeleton. Cytoskeletal components have been shown to play a major role in the maintenance of the nervous system through adulthood, and changes in neurofilaments and microtubule-associated proteins (MAPs) have been linked to a variety of neurodegenerative diseases. Here we show that Futsch, the fly homolog of MAP1B, is involved in progressive neurodegeneration. Although Futsch is widely expressed throughout the CNS, degeneration in futsch(olk) primarily occurs in the olfactory system and mushroom bodies. Consistent with the predicted function of Futsch, we find abnormalities in the microtubule network and defects in axonal transport. Degeneration in the adult brain is preceded by learning deficits, revealing a neuronal dysfunction before detectable levels of cell death. Futsch is negatively regulated by the Drosophila Fragile X mental retardation gene, and a mutation in this gene delays the onset of neurodegeneration in futsch(olk). A similar effect is obtained by expression of either fly or bovine tau, suggesting a certain degree of functional redundancy of MAPs. The futsch(olk) mutants exhibit several characteristics of human neurodegenerative diseases, providing an opportunity to study the role of MAPs in progressive neurodegeneration within an experimentally accessible, in vivo model system.",
    	author = {{Bettencourt da Cruz}, Alexandre and Schw\"{a}rzel, Martin and Schulze, Sabine and Niyyati, Mahtab and Heisenberg, Martin and Kretzschmar, Doris},
    	doi = "10.1091/mbc.E04-11-1004",
    	file = ":C$\backslash$:/Users/riku/AppData/Local/Mendeley Ltd./Mendeley Desktop/Downloaded/Bettencourt da Cruz et al. - 2005 - Disruption of the MAP1B-related protein FUTSCH leads to changes in the neuronal cytoskeleton, axonal.pdf:pdf",
    	issn = "1059-1524",
    	journal = "Molecular biology of the cell",
    	keywords = "Animals,Animals, Genetically Modified,Axonal Transport,Cattle,Cytoskeleton,Cytoskeleton: physiology,Drosophila,Drosophila Proteins,Drosophila Proteins: genetics,Drosophila Proteins: physiology,Drosophila: genetics,Drosophila: physiology,Female,Fragile X Mental Retardation Protein,Genes, Insect,Male,Microtubule-Associated Proteins,Microtubule-Associated Proteins: genetics,Microtubule-Associated Proteins: physiology,Mitochondria,Mitochondria: metabolism,Mutation,Nerve Degeneration,Nerve Degeneration: genetics,Nerve Degeneration: physiopathology,Nerve Growth Factors,Nerve Growth Factors: genetics,Nerve Growth Factors: physiology,Neurons,Neurons: physiology,RNA-Binding Proteins,RNA-Binding Proteins: genetics,RNA-Binding Proteins: physiology,Smell,Smell: genetics,Smell: physiology,tau Proteins,tau Proteins: genetics,tau Proteins: physiology",
    	month = "",
    	number = 5,
    	pages = "2433--42",
    	pmid = 15772149,
    	title = "{Disruption of the MAP1B-related protein FUTSCH leads to changes in the neuronal cytoskeleton, axonal transport defects, and progressive neurodegeneration in Drosophila.}",
    	url = "http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1087247\&tool=pmcentrez\&rendertype=abstract",
    	volume = 16,
    	year = 2005
    }