Excitatory synapse formation by trans-synaptic adhesions between NGL-3 and receptor protein tyrosine phosphatases LAR, PTPdelta, and PTPsigma = NGL-3와 receptor protein tyrosine phosphatase인 LAR, PTPdelta, PTPsigma의 상호작용에 의한 흥분성 시냅스 형성에 관한 연구

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dc.contributor.advisorKim, Eun-Joon-
dc.contributor.advisor김은준-
dc.contributor.authorKwon, Seok-Kyu-
dc.contributor.author권석규-
dc.date.accessioned2011-12-12T07:56:13Z-
dc.date.available2011-12-12T07:56:13Z-
dc.date.issued2010-
dc.identifier.urihttp://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=455357&flag=dissertation-
dc.identifier.urihttp://hdl.handle.net/10203/27706-
dc.description학위논문(박사) - 한국과학기술원 : 생명과학과, 2010.08, [ vi, 67 p. ]-
dc.description.abstractSynaptic cell adhesion molecules have been involved in the control of various aspects of synaptic development. Some known synaptic adhesion molecules bind trans-synaptically and heterophilically, and regulate the synapse formation in diverse synapses. I studied that NGL-3, a PSD-95-interacting postsynaptic adhesion molecule, and LAR, a receptor protein tyrosine phosphatase, expressed in heterologous cells induce pre- and postsynaptic differentiation in contacting axons and dendrites of cocultured rat hippocampal neurons, respectively. Neuronal over expression of NGL-3 increases presynaptic contacts on dendrites of transfected neurons. Knockdown of NGL-3 reduces excitatory synapses. Competitive inhibition by soluble LAR reduces NGL-3-induced presynaptic differentiation. The first two FNIII domains of LAR are molecular determinant for interacting with NGL-3, and the other LAR family members, PTP$\delta$ and PTP$\sigma$, also can bind to NGL-3 via first two FNIII domains. These two interactions promote synapse formation in a different manner; the PTP$\sigma$-NGL-3 interaction promotes synapse formation in a bidirectional manner, whereas the PTP$\delta$-NGL-3 interaction instructs only presynaptic differentiation in a unidirectional manner. mRNAs encoding LAR family proteins display overlapping and differential expression patterns in various brain regions. These results suggest that trans-synaptic adhesion between NGL-3 and the three LAR family proteins regulates excitatory synapse formation in shared and distinct neural circuits.eng
dc.languageeng-
dc.publisher한국과학기술원-
dc.subject피티피시그마-
dc.subject피티피델타-
dc.subject-
dc.subject엔지엘-
dc.subject시냅스-
dc.subjectsynapse-
dc.subjectPTPsigma-
dc.subjectPTPdelta-
dc.subjectLAR-
dc.subjectNGL-
dc.titleExcitatory synapse formation by trans-synaptic adhesions between NGL-3 and receptor protein tyrosine phosphatases LAR, PTPdelta, and PTPsigma = NGL-3와 receptor protein tyrosine phosphatase인 LAR, PTPdelta, PTPsigma의 상호작용에 의한 흥분성 시냅스 형성에 관한 연구-
dc.typeThesis(Ph.D)-
dc.identifier.CNRN455357/325007 -
dc.description.department한국과학기술원 : 생명과학과, -
dc.identifier.uid020057034-
dc.contributor.localauthorKim, Eun-Joon-
dc.contributor.localauthor김은준-
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