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Details on Person Seven in absentia homolog 1 (SIAH1) and 2 (SIAH2) are E3 ubi...
| Class:Id | Summation:5658515 |
|---|---|
| _displayName | Seven in absentia homolog 1 (SIAH1) and 2 (SIAH2) are E3 ubi... |
| _timestamp | 2015-03-26 10:33:16 |
| created | [InstanceEdit:5658493] Jupe, Steve, 2014-12-19 |
| literatureReference | [LiteratureReference:5658575] Siah-1 facilitates ubiquitination and degradation of synphilin-1 [LiteratureReference:5660758] Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease [LiteratureReference:5658576] Ubiquitination of alpha-synuclein by Siah-1 promotes alpha-synuclein aggregation and apoptotic cell death [LiteratureReference:5658554] Ubiquitination of alpha-synuclein and autophagy in Parkinson's disease |
| modified | [InstanceEdit:5660750] Jupe, Steve, 2015-01-06 [InstanceEdit:5667113] Jupe, Steve, 2015-01-23 [InstanceEdit:5685190] Jupe, Steve, 2015-03-26 |
| text | Seven in absentia homolog 1 (SIAH1) and 2 (SIAH2) are E3 ubiquitin-protein ligases that mediates ubiquitination of a number of target proteins including Synphilin-1 (SNCAIP) (Nagano et al. 2003) and alpha-synuclein (SNCA) (Liani et al. 2004, Lee et al. 2008). Ubiquitination of SNCA by SIAH1 is disrupted by the Parkinson's Disease (PD)-linked A30P mutation but not by the A53T mutation. SIAH1 binds the E2 ubiquitin-conjugating enzyme UBE2L6 (UBCH8) (Lee et al. 2008). This facilitates the mono- and di-ubiquitination of SNCA in vivo, but does not target SNCA for proteasomal degradation, rather it promotes SNCA aggregation and enhances toxicity (Lee et al. 2008). Monoubiquitinated SNCA may work as a seed for aggregation (Engelender 2008) and recruit other PD-related proteins, such as SNCAIP and UCHL1. |
| (summation) | [Reaction:5658496] SIAH1:UBE2L6:Ubiquitin binds SNCA [Homo sapiens] |
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No pathways have been reviewed or authored by Seven in absentia homolog 1 (SIAH1) and 2 (SIAH2) are E3 ubi... (5658515)
