DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Kim, Eun-Joon | - |
dc.contributor.advisor | 김은준 | - |
dc.contributor.author | Kwon, Seok-Kyu | - |
dc.contributor.author | 권석규 | - |
dc.date.accessioned | 2011-12-12T07:56:13Z | - |
dc.date.available | 2011-12-12T07:56:13Z | - |
dc.date.issued | 2010 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=455357&flag=dissertation | - |
dc.identifier.uri | http://hdl.handle.net/10203/27706 | - |
dc.description | 학위논문(박사) - 한국과학기술원 : 생명과학과, 2010.08, [ vi, 67 p. ] | - |
dc.description.abstract | Synaptic 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.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | 피티피시그마 | - |
dc.subject | 피티피델타 | - |
dc.subject | 라 | - |
dc.subject | 엔지엘 | - |
dc.subject | 시냅스 | - |
dc.subject | synapse | - |
dc.subject | PTPsigma | - |
dc.subject | PTPdelta | - |
dc.subject | LAR | - |
dc.subject | NGL | - |
dc.title | Excitatory synapse formation by trans-synaptic adhesions between NGL-3 and receptor protein tyrosine phosphatases LAR, PTPdelta, and PTPsigma | - |
dc.title.alternative | NGL-3와 receptor protein tyrosine phosphatase인 LAR, PTPdelta, PTPsigma의 상호작용에 의한 흥분성 시냅스 형성에 관한 연구 | - |
dc.type | Thesis(Ph.D) | - |
dc.identifier.CNRN | 455357/325007 | - |
dc.description.department | 한국과학기술원 : 생명과학과, | - |
dc.identifier.uid | 020057034 | - |
dc.contributor.localauthor | Kim, Eun-Joon | - |
dc.contributor.localauthor | 김은준 | - |
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