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    The schizophrenia susceptibility gene dysbindin controls synaptic homeostasis (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: The molecular mechanisms that achieve homeostatic stabilization of neural function remain largely unknown. To better understand how neural function is stabilized during development and throughout life, we used an electrophysiology-based forward genetic screen and assessed the function of more than 250 neuronally expressed genes for a role in the homeostatic modulation of synaptic transmission in Drosophila. This screen ruled out the involvement of numerous synaptic proteins and identified a critical function for dysbindin, a gene linked to schizophrenia in humans. We found that dysbindin is required presynaptically for the retrograde, homeostatic modulation of neurotransmission, and functions in a dose-dependent manner downstream or independently of calcium influx. Thus, dysbindin is essential for adaptive neural plasticity and may link altered homeostatic signaling with a complex neurological disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3063306/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3063306/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dickman, Dion K -- Davis, Graeme W -- NS39313/NS/NINDS NIH HHS/ -- R01 NS039313/NS/NINDS NIH HHS/ -- R01 NS039313-12/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2009 Nov 20;326(5956):1127-30. doi: 10.1126/science.1179685.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965435" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium Channels/genetics/metabolism ; Carrier Proteins/genetics ; Drosophila Proteins/genetics/metabolism ; Drosophila melanogaster/*genetics/*physiology ; Dystrophin-Associated Proteins ; Genes, Insect ; Glutamic Acid/metabolism ; Homeostasis ; Humans ; Mutation ; Neuromuscular Junction/physiology ; Neuronal Plasticity ; Schizophrenia/genetics ; Synapses/*physiology/ultrastructure ; *Synaptic Transmission ; Synaptic Vesicles/metabolism ; Transgenes
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Proteasomal regulation of the hypoxic response modulates aging in C. elegans (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-18
    Description: The Caenorhabditis elegans von Hippel-Lindau tumor suppressor homolog VHL-1 is a cullin E3 ubiquitin ligase that negatively regulates the hypoxic response by promoting ubiquitination and degradation of the hypoxic response transcription factor HIF-1. Here, we report that loss of VHL-1 significantly increased life span and enhanced resistance to polyglutamine and beta-amyloid toxicity. Deletion of HIF-1 was epistatic to VHL-1, indicating that HIF-1 acts downstream of VHL-1 to modulate aging and proteotoxicity. VHL-1 and HIF-1 control longevity by a mechanism distinct from both dietary restriction and insulin-like signaling. These findings define VHL-1 and the hypoxic response as an alternative longevity and protein homeostasis pathway.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2737476/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2737476/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mehta, Ranjana -- Steinkraus, Katherine A -- Sutphin, George L -- Ramos, Fresnida J -- Shamieh, Lara S -- Huh, Alexander -- Davis, Christina -- Chandler-Brown, Devon -- Kaeberlein, Matt -- 1R01AG031108-01/AG/NIA NIH HHS/ -- P30AG013280/AG/NIA NIH HHS/ -- R01 AG031108/AG/NIA NIH HHS/ -- R01 AG031108-01A1/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2009 May 29;324(5931):1196-8. doi: 10.1126/science.1173507. Epub 2009 Apr 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19372390" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*physiology ; Amyloid beta-Peptides/toxicity ; Animals ; Caenorhabditis elegans/genetics/metabolism/*physiology ; Caenorhabditis elegans Proteins/genetics/*metabolism ; Caloric Restriction ; Cullin Proteins/genetics/*metabolism ; Female ; Fertility ; Gene Expression Regulation ; Homeostasis ; Insulin/metabolism ; Longevity/physiology ; Male ; Models, Animal ; Oxygen/*physiology ; Peptides/toxicity ; Proteasome Endopeptidase Complex/*metabolism ; RNA Interference ; Receptor, Insulin/genetics/metabolism ; Signal Transduction ; Transcription Factors/genetics/*metabolism ; Ubiquitination
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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