Role of the E3 ubiquitin ligase dorfin in the degradation of PSD-95 family proteins = E3 ubiquitin ligase dorfin에 의한 PSD-95 분해에 관한 연구

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The post synaptic density (PSD) is a postsynaptic membrane specialization at neuronal synapses. The PSD undergoes dynamic structural changes and protein turnover during synaptic maturation and plasticity. A key mechanism controlling protein turnover is the ubiquitin-proteasome pathway. Here I identified Dorfin, a RING finger-type E3 ubiquitin ligase, as a binding partner of PSD-95, an abundant PSD component that is important for synaptic structure and plasticity. The C terminus of Dorfin interacts with the PDZ domains of PSD-95. Dorfin selectively binds to the PSD-95 family proteins as shown in yeast two-hybrid, coimmunoprecipitation and coclustering assays. Dorfin selectively ubiquitinates PSD-95 and other PSD-95 family proteins. These results suggest that Dorfin, through the degradation of PSD-95 family proteins, contributes to the structural and functional plasticity of synapses.
Advisors
Chung, Jae-Hoonresearcher정재훈researcher
Description
한국과학기술원 : 생명과학과,
Publisher
한국과학기술원
Issue Date
2004
Identifier
240340/325007  / 020023931
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생명과학과, 2004, [ iv, 54 p. ]

Keywords

DORFIN; E3 UBIQUITIN LIGASE; PSD-95; PSD-95 분해; Dorfin; E3 ubiquitin 연결 효소; DEGRADATION

URI
http://hdl.handle.net/10203/28035
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=240340&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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