Document Detail


CYY-1/cyclin Y and CDK-5 differentially regulate synapse elimination and formation for rewiring neural circuits.
MedLine Citation:
PMID:  21609829     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The assembly and maturation of neural circuits require a delicate balance between synapse formation and elimination. The cellular and molecular mechanisms that coordinate synaptogenesis and synapse elimination are poorly understood. In C. elegans, DD motoneurons respecify their synaptic connectivity during development by completely eliminating existing synapses and forming new synapses without changing cell morphology. Using loss- and gain-of-function genetic approaches, we demonstrate that CYY-1, a cyclin box-containing protein, drives synapse removal in this process. In addition, cyclin-dependent kinase-5 (CDK-5) facilitates new synapse formation by regulating the transport of synaptic vesicles to the sites of synaptogenesis. Furthermore, we show that coordinated activation of UNC-104/Kinesin3 and Dynein is required for patterning newly formed synapses. During the remodeling process, presynaptic components from eliminated synapses are recycled to new synapses, suggesting that signaling mechanisms and molecular motors link the deconstruction of existing synapses and the assembly of new synapses during structural synaptic plasticity.
Authors:
Mikyoung Park; Shigeki Watanabe; Vivian Yi Nuo Poon; Chan-Yen Ou; Erik M Jorgensen; Kang Shen
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Neuron     Volume:  70     ISSN:  1097-4199     ISO Abbreviation:  Neuron     Publication Date:  2011 May 
Date Detail:
Created Date:  2011-05-25     Completed Date:  2011-08-16     Revised Date:  2012-12-04    
Medline Journal Info:
Nlm Unique ID:  8809320     Medline TA:  Neuron     Country:  United States    
Other Details:
Languages:  eng     Pagination:  742-57     Citation Subset:  IM    
Copyright Information:
Copyright © 2011 Elsevier Inc. All rights reserved.
Affiliation:
Department of Biology, Stanford University, CA 94305, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins / physiology*
Cyclin-Dependent Kinase 5 / physiology*
Cyclins / physiology*
Nerve Net / physiology*
Neuronal Plasticity / physiology*
Synapses / physiology*
Grant Support
ID/Acronym/Agency:
5R01 NS048392/NS/NINDS NIH HHS; R01 NS034307-18/NS/NINDS NIH HHS; R01 NS048392/NS/NINDS NIH HHS; R01 NS048392-07/NS/NINDS NIH HHS; //Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/CCNY protein, human; 0/Caenorhabditis elegans Proteins; 0/Cyclins; EC 2.7.11.22/Cyclin-Dependent Kinase 5

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