Trans-synaptic mechanism of retinal synapse formation and function
视网膜突触形成和功能的跨突触机制
基本信息
- 批准号:10621537
- 负责人:
- 金额:--
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2019
- 资助国家:美国
- 起止时间:2019-09-01 至 2022-08-31
- 项目状态:已结题
- 来源:
- 关键词:AdhesionsAdoptedAdvanced DevelopmentAffectAffinityAxonBindingCalcium ChannelCell Adhesion MoleculesComplexConeCone dystrophyCouplesDeletion MutagenesisDevelopmentElectrophysiology (science)ElectroporationGoalsIn VitroInner Plexiform LayerLeucine-Rich RepeatMediatingMentorsMolecularMorphologyNeural RetinaNeuronsNight BlindnessPathologyPhasePhotoreceptorsPlayProteinsReceptor SignalingReportingResearchRetinaRetinal DiseasesRodRoleSiteSynapsesSynaptic ReceptorsTechniquesTestingTransplantationWorkbasecell typeextracellularin vivoinformation processinginnovationinsightleucine-rich repeat proteinmutantneural circuitneurotransmitter releasereceptorretinal neuronretinal rodsribbon synapsesynaptic functionsynaptogenesistherapeutic developmenttraffickingtransplantation therapyvisual informationvisual performance
项目摘要
PROJECT SUMMARY/ABSTRACT
Our optimal visual performance starts with the correct parallel visual information processing in the retina
which depends on precise retinal neural circuit formation. To achieve this, retinal neurons must accurately set
up functional synapses which require precise alignment between the pre-synaptic neurotransmitter releasing site
and the post-synaptic receptor. Increasing evidence suggests that cell adhesion molecules (CAMs)-mediated
trans-synaptic complexes are critical for synapse formation and function, however, the mechanism how pre-
synaptic releasing machinery coordinates with the post-synaptic receptor signaling complex at retinal ribbon
synapses is largely unknown. We recently reported that the extracellular calcium channel auxiliary subunit α2δ4
is necessary for rod photoreceptor axonal elaboration and synapse formation and demonstrated that α2δ4 does
so through controlling the synaptic targeting of ELFN1, a leucine-rich repeat (LRR) protein specifically expressed
at rod synapse and interacts trans-synaptically with the post-synaptic mGluR6 receptor. We also showed that
α2δ4 interacts with ELFN1 through the LRR domain, a conserved domain shared across many LRR proteins.
Interestingly, we and other lab identified another LRR protein termed LRIT1, which specifically affects cone
synaptic function. The objective of the proposed work is to determine whether it is a general mechanism that
pre-synaptic calcium channel complex utilizes α2δ4 to coordinate with post-synaptic receptor through the
facilitation of different LRR proteins. In Aim 1, we will determine the functional role of α2δ4-ELFN1 interaction in
rod synapse formation using in vivo electroporation combined with deletion mutagenesis. In Aim 2, we will study
how LRIT1 regulates cone synaptic function by testing whether LRIT1 affects pre-synaptic Cav1.4 channel
activity through α2δ4 using electrophysiological recording. In Aim 3, I will investigate whether synapses in the
inner plexiform layer (IPL) also adopt similar trans-synaptic mechanism by studying how α2δ4 and LRIT1 affect
RBC-AII amacrine synapse formation and function using the technique gained during the mentored phase. This
proposal is innovative because no mechanistic studies has been done on α2δ4 protein despite its clearly
important role in photoreceptor synapse formation and function. The proposed work is significant since results
from this study will enable better understanding of how retinal neurons establish and maintain synaptic contact.
项目总结/文摘
项目成果
期刊论文数量(0)
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科研奖励数量(0)
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专利数量(0)
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Yuchen Wang其他文献
Yuchen Wang的其他文献
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{{ truncateString('Yuchen Wang', 18)}}的其他基金
Trans-synaptic mechanism of retinal synapse formation and function
视网膜突触形成和功能的跨突触机制
- 批准号:
10682742 - 财政年份:2019
- 资助金额:
-- - 项目类别:
Trans-synaptic mechanism of retinal synapse formation and function
视网膜突触形成和功能的跨突触机制
- 批准号:
10426669 - 财政年份:2019
- 资助金额:
-- - 项目类别:
Trans-synaptic mechanism of retinal synapse formation and function
视网膜突触形成和功能的跨突触机制
- 批准号:
9806146 - 财政年份:2019
- 资助金额:
-- - 项目类别:
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