项目来源

韩国国家研究基金(NRF)

项目主持人

정상용

项目受资助机构

포항공과대학교

项目编号

2009-352-H00008

立项年度

2009

立项时间

未公开

项目级别

国家级

研究期限

未知 / 未知

受资助金额

未知

学科

복합학

学科代码

未公开

基金类别

人文社科-SD-Research

关键词

시냅스 가소성 ; 세포점착 단백질 ; 동물 행동 기억 ; 시냅스 점착 단백질(synaptic adhesion protein) ; 신경전달물질 분비(synaptic vesicle release) ; Neurexin ; autism ; synaptic plasticity ; Synaptotagmin ; neuroligin ; synaptotagmin ; axon terminal

参与者

정상용

参与机构

未公开

项目标书摘要：Research Summary:Synapse formation,maturation and synaptic transmission are driven by many synaptic adhesion proteins.NRX/NL complexs are well known as a heterotypic interaction in neurons.NRX and NL have many spicing alternative variants that enable bidirectional signaling in synaptic clefts and to control specific synapse formation in brain.βNRX can bind to presynaptic proteins such as synaptotagmin1(syt1),CASK,Mint,and Lin 7.Syt1 is known to act as calcium sensor during synaptic vesicle(SV)fusion.However,the physiological function of NRXs is not still known in presynaptic terminal.To address the function of NRXs,I used the autaptic culture system that has mainly used to dissect the neurotransmitter release in neurons.This system enables to measure the vesicle release probability and readily releasable pool in detail.Given that syt1 binds with NRXs,the function of sy1 is important factor to dissect the function of NRX.Syt1 acts as a calcium sensor and fusion accelerator.According to the results,NRXs may function via NLs or other interacting proteins in postsynaptic adhesion proteins.In the case of NL1/2/3 KO,the synapse formation and density of spine are not impaired.This result makes NL4 to be more important protein in brain functions.NL4 was mainly expressed in stratum lacunosom moleculare but the expression was not strong than other NLs and mainly expressed in excitatory synapse.The amplitude and frequency of mEPSC were not different.On the base of these results,βNRX may function as a bidirectional player in pre-and postsynanptic neurons.

Application Abstract: Research Summary:Synapse formation,maturation and synaptic transmission are driven by many synaptic adhesion proteins.NRX/NL complexs are well known as a heterotypic interaction in neurons.NRX and NL have many spicing alternative variants that enable bidirectional signaling in synaptic clefts and to control specific synapse formation in brain.βNRX can bind to presynaptic proteins such as synaptotagmin1(syt1),CASK,Mint,and Lin 7.Syt1 is known to act as calcium sensor during synaptic vesicle(SV)fusion.However,the physiological function of NRXs is not still known in presynaptic terminal.To address the function of NRXs,I used the autaptic culture system that has mainly used to dissect the neurotransmitter release in neurons.This system enables to measure the vesicle release probability and readily releasable pool in detail.Given that syt1 binds with NRXs,the function of sy1 is important factor to dissect the function of NRX.Syt1 acts as a calcium sensor and fusion accelerator.According to the results,NRXs may function via NLs or other interacting proteins in postsynaptic adhesion proteins.In the case of NL1/2/3 KO,the synapse formation and density of spine are not impaired.This result makes NL4 to be more important protein in brain functions.NL4 was mainly expressed in stratum lacunosom moleculare but the expression was not strong than other NLs and mainly expressed in excitatory synapse.The amplitude and frequency of mEPSC were not different.On the base of these results,βNRX may function as a bidirectional player in pre-and postsynanptic neurons.