Synaptic Protein Degradation in Memory Reorganization
The ubiquitin-proteasome system (UPS) is a ubiquitous, major pathway of protein degradation that is involved in most cellular processes by regulating the abundance of certain proteins. Accumulating evidence indicates a role for the UPS in specific functio
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Synaptic Protein Degradation in Memory Reorganization Bong-Kiun Kaang and Jun-Hyeok Choi
Abstract The ubiquitin-proteasome system (UPS) is a ubiquitous, major pathway of protein degradation that is involved in most cellular processes by regulating the abundance of certain proteins. Accumulating evidence indicates a role for the UPS in specific functions of neurons. In this chapter, we first introduce the role of the UPS in neuronal function and the mechanism of UPS regulation following synaptic activity. Then, we focus on the recently revealed, distinct role of the UPS in the destabilization of a reactivated memory. Finally, we discuss the physiological role of this destabilization process. The reactivated memory may undergo modification from the initial memory depending on the context in which the memory is reactivated, which we will term memory reorganization. We will introduce the role of the protein degradation–dependent destabilization process for memory reorganization and suggest a hypothetical model combining the recent findings. Keywords E3 ubiquitin ligase • Long-term memory • Spine • Ubiquitin proteasome system
B.-K. Kaang (*) National Creative Research Initiative Center for Memory, Department of Biological Sciences, College of Natural Sciences, Seoul National University, 151-742 Seoul, South Korea Department of Brain and Cognitive Sciences, College of Natural Sciences, Seoul National University, 151-742 Seoul, South Korea e-mail: [email protected] J.-H. Choi National Creative Research Initiative Center for Memory, Department of Biological Sciences, College of Natural Sciences, Seoul National University, 151-742 Seoul, South Korea e-mail: [email protected] M.R. Kreutz and C. Sala (eds.), Synaptic Plasticity, Advances in Experimental Medicine and Biology 970, DOI 10.1007/978-3-7091-0932-8_10, # Springer-Verlag/Wien 2012
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B.-K. Kaang and J.-H. Choi
Introduction
The ubiquitin-proteasome system (UPS) is a ubiquitous, major pathway of protein degradation that governs the turnover of proteins, thereby inevitably affecting every process in which proteins are involved. In the UPS, the small protein ubiquitin is covalently conjugated to a substrate protein by the serial action of the E1 ubiquitinactivating enzyme, the E2 ubiquitin-conjugating enzyme, and the E3 ubiquitin ligase. After a serial reaction to produce a polyubiquitin chain on the substrate, the polyubiquitinated substrate is directed to a large proteasome complex that manages the degradation. E3 ubiquitin ligase seems to be the major component that determines substrate specificity (Fig. 10.1). Emerging evidence indicates the critical involvement of protein degradation in specialized functions of the neurons. Ubiquitin-proteasome-dependent degradation is known to play important roles in the regulation of synaptogenesis and the elimination of synapses in the development (DiAntonio et al. 2001; Ding et al. 2007; Liao et al. 2004; Schaefer et al. 2000; van Roessel et al. 2004; Wan et al. 2000), maintenance, and modulation of neurotransm
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