Document Detail


Nicotinamide mononucleotide adenylyltransferase maintains active zone structure by stabilizing Bruchpilot.
MedLine Citation:
PMID:  23154466     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Active zones are specialized presynaptic structures critical for neurotransmission. We show that a neuronal maintenance factor, nicotinamide mononucleotide adenylyltransferase (NMNAT), is required for maintaining active zone structural integrity in Drosophila by interacting with the active zone protein, Bruchpilot (BRP), and shielding it from activity-induced ubiquitin-proteasome-mediated degradation. NMNAT localizes to the peri-active zone and interacts biochemically with BRP in an activity-dependent manner. Loss of NMNAT results in ubiquitination, mislocalization and aggregation of BRP, and subsequent active zone degeneration. We propose that, as a neuronal maintenance factor, NMNAT specifically maintains active zone structure by direct protein-protein interaction.
Authors:
Shaoyun Zang; Yousuf O Ali; Kai Ruan; R Grace Zhai
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-11-16
Journal Detail:
Title:  EMBO reports     Volume:  14     ISSN:  1469-3178     ISO Abbreviation:  EMBO Rep.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-03     Completed Date:  2013-06-03     Revised Date:  2014-01-09    
Medline Journal Info:
Nlm Unique ID:  100963049     Medline TA:  EMBO Rep     Country:  England    
Other Details:
Languages:  eng     Pagination:  87-94     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Drosophila / enzymology,  genetics*
Drosophila Proteins / genetics*,  metabolism
Gene Expression Regulation
Nicotinamide-Nucleotide Adenylyltransferase / antagonists & inhibitors,  genetics*,  metabolism
Presynaptic Terminals / enzymology*,  ultrastructure
Proteasome Endopeptidase Complex
Protein Binding
Proteolysis
RNA, Small Interfering / genetics
Signal Transduction
Synaptic Transmission / physiology
Ubiquitin / genetics,  metabolism
Ubiquitination
Grant Support
ID/Acronym/Agency:
1R01NS064269/NS/NINDS NIH HHS; R01 NS064269/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Drosophila Proteins; 0/RNA, Small Interfering; 0/Ubiquitin; 0/bruchpilot protein, Drosophila; EC 2.7.7.1/Nicotinamide-Nucleotide Adenylyltransferase; EC 3.4.25.1/Proteasome Endopeptidase Complex
Comments/Corrections
Comment In:
EMBO Rep. 2013 Jan;14(1):5-6   [PMID:  23196365 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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