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- W2004134367 abstract "Many pathways important to the nervous system are regulated by the post-translational conjugation of ubiquitin to target proteins. The reversal of ubiquitination, or deubiquitination, is equally critical to neuronal function. By countering protein ubiquitination, deubiquitinating enzymes (DUBs) help control neuronal fate determination, axonal pathfinding and synaptic communication and plasticity. The significance of DUBs to the nervous system is underscored by links to various neurological diseases. Owing to cell type or substrate specificity, certain DUBs might also represent therapeutic targets for neurodegeneration. Here, we review recent findings that have shaped our current understanding of emerging functions for DUBs in the nervous system. Many pathways important to the nervous system are regulated by the post-translational conjugation of ubiquitin to target proteins. The reversal of ubiquitination, or deubiquitination, is equally critical to neuronal function. By countering protein ubiquitination, deubiquitinating enzymes (DUBs) help control neuronal fate determination, axonal pathfinding and synaptic communication and plasticity. The significance of DUBs to the nervous system is underscored by links to various neurological diseases. Owing to cell type or substrate specificity, certain DUBs might also represent therapeutic targets for neurodegeneration. Here, we review recent findings that have shaped our current understanding of emerging functions for DUBs in the nervous system. gross lack of coordination. A neurological symptom that usually indicates a dysfunction of neural pathways involved in motor coordination. a family of cysteine and metallo-proteases that cleave chemical bonds between ubiquitin molecules or between ubiquitin and another protein. ubiquitin–ubiquitin linkages that generally target substrate proteins for degradation by the proteasome. ubiquitin-ubiquitin linkages that generally target proteins in non-degradative pathways. ubiquitin conjugation that involves a single moiety of ubiquitin. This type of ubiquitination can alter the sub-cellular localization of a protein and regulate cellular processes such as receptor trafficking and gene transcription. ubiquitin conjugation that involves chains of >1 ubiquitin moiety. A variety of different types of ubiquitin chains are known (e.g. K6, K11, K27, K29, K33, K48 and K63-linked ubiquitin chains). a large molecular complex found in all eukaryotic cells, the proteasome selectively degrades poly-ubiquitinated proteins. It consists of the 20S particle, which proteolyses proteins and one or two regulatory 19S particles. a small regulatory protein that alters the interaction properties of proteins to which it is conjugated." @default.
- W2004134367 created "2016-06-24" @default.
- W2004134367 creator A5015909717 @default.
- W2004134367 creator A5055180300 @default.
- W2004134367 date "2011-07-01" @default.
- W2004134367 modified "2023-10-18" @default.
- W2004134367 title "Balancing act: deubiquitinating enzymes in the nervous system" @default.
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