LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 5 of total 5

Search options

  1. Article ; Online: Rich regulates target specificity of photoreceptor cells and N-cadherin trafficking in the Drosophila visual system via Rab6.

    Tong, Chao / Ohyama, Tomoko / Tien, An-Chi / Rajan, Akhila / Haueter, Claire M / Bellen, Hugo J

    Neuron

    2011  Volume 71, Issue 3, Page(s) 447–459

    Abstract: Neurons establish specific synaptic connections with their targets, a process that is highly regulated. Numerous cell adhesion molecules have been implicated in target recognition, but how these proteins are precisely trafficked and targeted is poorly ... ...

    Abstract Neurons establish specific synaptic connections with their targets, a process that is highly regulated. Numerous cell adhesion molecules have been implicated in target recognition, but how these proteins are precisely trafficked and targeted is poorly understood. To identify components that affect synaptic specificity, we carried out a forward genetic screen in the Drosophila eye. We identified a gene, named ric1 homologue (rich), whose loss leads to synaptic specificity defects. Loss of rich leads to reduction of N-Cadherin in the photoreceptor cell synapses but not of other proteins implicated in target recognition, including Sec15, DLAR, Jelly belly, and PTP69D. The Rich protein binds to Rab6, and Rab6 mutants display very similar phenotypes as the rich mutants. The active form of Rab6 strongly suppresses the rich synaptic specificity defect, indicating that Rab6 is regulated by Rich. We propose that Rich activates Rab6 to regulate N-Cadherin trafficking and affects synaptic specificity.
    MeSH term(s) Animals ; Cadherins/metabolism ; Drosophila ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Mutation ; Photoreceptor Cells, Invertebrate/metabolism ; Photoreceptor Cells, Invertebrate/physiology ; Signal Transduction/physiology ; Synapses/genetics ; Synapses/metabolism ; Synapses/physiology ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism ; ras Proteins/genetics ; ras Proteins/metabolism
    Chemical Substances Cadherins ; Drosophila Proteins ; RIC protein, Drosophila ; Rab6 protein ; rab GTP-Binding Proteins (EC 3.6.5.2) ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2011-07-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 808167-0
    ISSN 1097-4199 ; 0896-6273
    ISSN (online) 1097-4199
    ISSN 0896-6273
    DOI 10.1016/j.neuron.2011.06.040
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2496: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 92: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: The Arp2/3 complex and WASp are required for apical trafficking of Delta into microvilli during cell fate specification of sensory organ precursors.

    Rajan, Akhila / Tien, An-Chi / Haueter, Claire M / Schulze, Karen L / Bellen, Hugo J

    Nature cell biology

    2009  Volume 11, Issue 7, Page(s) 815–824

    Abstract: Cell fate decisions mediated by the Notch signalling pathway require direct cell-cell contact between adjacent cells. In Drosophila melanogaster, an external sensory organ (ESO) develops from a single sensory organ precursor (SOP) and its fate ... ...

    Abstract Cell fate decisions mediated by the Notch signalling pathway require direct cell-cell contact between adjacent cells. In Drosophila melanogaster, an external sensory organ (ESO) develops from a single sensory organ precursor (SOP) and its fate specification is governed by differential Notch activation. Here we show that mutations in actin-related protein-3 (Arp3) compromise Notch signalling, leading to a fate transformation of the ESO. Our data reveal that during ESO fate specification, most endocytosed vesicles containing the ligand Delta traffic to a prominent apical actin-rich structure (ARS) formed in the SOP daughter cells. Using immunohistochemistry and transmission electron microscopy (TEM) analyses, we show that the ARS contains numerous microvilli on the apical surface of SOP progeny. In Arp2/3 and WASp mutants, the surface area of the ARS is substantially reduced and there are significantly fewer microvilli. More importantly, trafficking of Delta-positive vesicles from the basal area to the apical portion of the ARS is severely compromised. Our data indicate that WASp-dependent Arp2/3 actin polymerization is crucial for apical presentation of Delta, providing a mechanistic link between actin polymerization and Notch signalling.
    MeSH term(s) Actin-Related Protein 2-3 Complex/genetics ; Actin-Related Protein 2-3 Complex/metabolism ; Actin-Related Protein 2-3 Complex/physiology ; Animals ; Biological Transport/genetics ; Biological Transport/physiology ; Blotting, Western ; Cell Differentiation/genetics ; Cell Differentiation/physiology ; Drosophila melanogaster/embryology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Drosophila melanogaster/ultrastructure ; Endocytosis/genetics ; Endocytosis/physiology ; Gene Expression Regulation, Developmental ; Immunohistochemistry ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins/metabolism ; Microscopy, Electron, Transmission ; Microscopy, Immunoelectron ; Microvilli/metabolism ; Microvilli/ultrastructure ; Sense Organs/embryology ; Sense Organs/metabolism ; Sense Organs/ultrastructure ; Wiskott-Aldrich Syndrome Protein/genetics ; Wiskott-Aldrich Syndrome Protein/metabolism ; Wiskott-Aldrich Syndrome Protein/physiology
    Chemical Substances Actin-Related Protein 2-3 Complex ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Wiskott-Aldrich Syndrome Protein ; delta protein
    Language English
    Publishing date 2009-06-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/ncb1888
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 5169: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 12: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: NAD synthase NMNAT acts as a chaperone to protect against neurodegeneration.

    Zhai, R Grace / Zhang, Fan / Hiesinger, P Robin / Cao, Yu / Haueter, Claire M / Bellen, Hugo J

    Nature

    2008  Volume 452, Issue 7189, Page(s) 887–891

    Abstract: Neurodegeneration can be triggered by genetic or environmental factors. Although the precise cause is often unknown, many neurodegenerative diseases share common features such as protein aggregation and age dependence. Recent studies in Drosophila have ... ...

    Abstract Neurodegeneration can be triggered by genetic or environmental factors. Although the precise cause is often unknown, many neurodegenerative diseases share common features such as protein aggregation and age dependence. Recent studies in Drosophila have uncovered protective effects of NAD synthase nicotinamide mononucleotide adenylyltransferase (NMNAT) against activity-induced neurodegeneration and injury-induced axonal degeneration. Here we show that NMNAT overexpression can also protect against spinocerebellar ataxia 1 (SCA1)-induced neurodegeneration, suggesting a general neuroprotective function of NMNAT. It protects against neurodegeneration partly through a proteasome-mediated pathway in a manner similar to heat-shock protein 70 (Hsp70). NMNAT displays chaperone function both in biochemical assays and cultured cells, and it shares significant structural similarity with known chaperones. Furthermore, it is upregulated in the brain upon overexpression of poly-glutamine expanded protein and recruited with the chaperone Hsp70 into protein aggregates. Our results implicate NMNAT as a stress-response protein that acts as a chaperone for neuronal maintenance and protection. Our studies provide an entry point for understanding how normal neurons maintain activity, and offer clues for the common mechanisms underlying different neurodegenerative conditions.
    MeSH term(s) Amide Synthases/genetics ; Amide Synthases/metabolism ; Animals ; Ataxin-1 ; Ataxins ; Brain/metabolism ; COS Cells ; Chlorocebus aethiops ; Disease Models, Animal ; Drosophila/enzymology ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Nerve Degeneration ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nerve Tissue Proteins/toxicity ; Neurodegenerative Diseases/enzymology ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/pathology ; Neurodegenerative Diseases/prevention & control ; Nicotinamide-Nucleotide Adenylyltransferase/genetics ; Nicotinamide-Nucleotide Adenylyltransferase/metabolism ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Nuclear Proteins/toxicity ; Spinocerebellar Ataxias/enzymology ; Spinocerebellar Ataxias/genetics ; Spinocerebellar Ataxias/pathology ; Spinocerebellar Ataxias/prevention & control
    Chemical Substances ATXN1 protein, human ; Ataxin-1 ; Ataxins ; Drosophila Proteins ; HSP70 Heat-Shock Proteins ; Molecular Chaperones ; Nerve Tissue Proteins ; Nuclear Proteins ; Nicotinamide-Nucleotide Adenylyltransferase (EC 2.7.7.1) ; Amide Synthases (EC 6.3.1.-) ; NAD+ synthase (EC 6.3.1.5)
    Language English
    Publishing date 2008-03-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/nature06721
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 26: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: A synaptic vesicle-associated Ca2+ channel promotes endocytosis and couples exocytosis to endocytosis.

    Yao, Chi-Kuang / Lin, Yong Qi / Ly, Cindy V / Ohyama, Tomoko / Haueter, Claire M / Moiseenkova-Bell, Vera Y / Wensel, Theodore G / Bellen, Hugo J

    Cell

    2009  Volume 138, Issue 5, Page(s) 947–960

    Abstract: Synaptic vesicle (SV) exo- and endocytosis are tightly coupled to sustain neurotransmission in presynaptic terminals, and both are regulated by Ca(2+). Ca(2+) influx triggered by voltage-gated Ca(2+) channels is necessary for SV fusion. However, ... ...

    Abstract Synaptic vesicle (SV) exo- and endocytosis are tightly coupled to sustain neurotransmission in presynaptic terminals, and both are regulated by Ca(2+). Ca(2+) influx triggered by voltage-gated Ca(2+) channels is necessary for SV fusion. However, extracellular Ca(2+) has also been shown to be required for endocytosis. The intracellular Ca(2+) levels (<1 microM) that trigger endocytosis are typically much lower than those (>10 microM) needed to induce exocytosis, and endocytosis is inhibited when the Ca(2+) level exceeds 1 microM. Here, we identify and characterize a transmembrane protein associated with SVs that, upon SV fusion, localizes at periactive zones. Loss of Flower results in impaired intracellular resting Ca(2+) levels and impaired endocytosis. Flower multimerizes and is able to form a channel to control Ca(2+) influx. We propose that Flower functions as a Ca(2+) channel to regulate synaptic endocytosis and hence couples exo- with endocytosis.
    MeSH term(s) Animals ; Calcium Channels/analysis ; Calcium Channels/metabolism ; Drosophila Proteins/analysis ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology ; Drosophila melanogaster/metabolism ; Endocytosis ; Exocytosis ; Protein Isoforms/analysis ; Protein Isoforms/metabolism ; Synaptic Vesicles/chemistry ; Synaptic Vesicles/metabolism
    Chemical Substances Calcium Channels ; Drosophila Proteins ; Protein Isoforms ; fwe protein, Drosophila
    Language English
    Publishing date 2009-09-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2009.06.033
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1167: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 58: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: The nuclear orphan receptor COUP-TFII plays an essential role in adipogenesis, glucose homeostasis, and energy metabolism.

    Li, Luoping / Xie, Xin / Qin, Jun / Jeha, George S / Saha, Pradip K / Yan, Jun / Haueter, Claire M / Chan, Lawrence / Tsai, Sophia Y / Tsai, Ming-Jer

    Cell metabolism

    2008  Volume 9, Issue 1, Page(s) 77–87

    Abstract: Adipose tissue development and function play a central role in the pathogenesis and pathophysiology of metabolic syndromes. Here, we show that chicken ovalbumin upstream promoter transcription factor II (COUP-TFII) plays a pivotal role in adipogenesis ... ...

    Abstract Adipose tissue development and function play a central role in the pathogenesis and pathophysiology of metabolic syndromes. Here, we show that chicken ovalbumin upstream promoter transcription factor II (COUP-TFII) plays a pivotal role in adipogenesis and energy homeostasis. COUP-TFII is expressed in the early stages of white adipocyte development. COUP-TFII heterozygous mice (COUP-TFII(+/-)) have much less white adipose tissue (WAT) than wild-type mice (COUP-TFII(+/+)). COUP-TFII(+/-) mice display a decreased expression of key regulators for WAT development. Knockdown COUP-TFII in 3T3-L1 cells resulted in an increased expression of Wnt10b, while chromatin immunoprecipitation analysis revealed that Wnt10b is a direct target of COUP-TFII. Moreover, COUP-TFII(+/-) mice have increased mitochondrial biogenesis in WAT, and COUP-TFII(+/-) mice have improved glucose homeostasis and increased energy expenditure. Thus, COUP-TFII regulates adipogenesis by regulating the key molecules in adipocyte development and can serve as a target for regulating energy metabolism.
    MeSH term(s) 3T3-L1 Cells ; Adipogenesis ; Adipose Tissue, White/metabolism ; Animals ; COUP Transcription Factor II/metabolism ; Cell Differentiation ; Chickens ; Energy Metabolism ; Female ; Gene Knockdown Techniques ; Glucose/metabolism ; Heterozygote ; Male ; Mice ; Mice, Knockout ; Obesity/etiology ; Obesity/prevention & control ; Time Factors ; Wnt Proteins/metabolism
    Chemical Substances COUP Transcription Factor II ; Wnt Proteins ; Wnt10b protein, mouse ; Glucose (IY9XDZ35W2)
    Language English
    Publishing date 2008-11-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2176834-1
    ISSN 1932-7420 ; 1550-4131
    ISSN (online) 1932-7420
    ISSN 1550-4131
    DOI 10.1016/j.cmet.2008.12.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6169: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top