Ub-SNCA dissociates from the conjugating enzyme

Stable Identifier
R-HSA-5660757
Type
Reaction [uncertain]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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Ub-SNCA dissociates from the conjugating enzyme
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SNCA is monoubiquitinated and under some circumstances released to accumulate in the cell. Alternatively Ub-SNCA may undergo further rounds of ubiquitination producing diubiquitinated or polyubiquitinated forms. The precise mechanism of release and subsequent further ubiquitination is unclear (Sadowski et al. 2011); the E3 ligase may remain bound to SNCA while the E2 ligase dissociates to be replaced by a Ubiquitin-associated replacement, or the E2/E3 complex may dissociate completely allowing a different E3 to bind the SNCA substrate.
Literature References
PubMed ID Title Journal Year
22131221 Protein monoubiquitination and polyubiquitination generate structural diversity to control distinct biological processes

Sadowski, M, Suryadinata, R, Tan, AR, Roesley, SN, Sarcevic, B

IUBMB Life 2012
18070888 Monoubiquitylation of alpha-synuclein by seven in absentia homolog (SIAH) promotes its aggregation in dopaminergic cells

Rott, R, Szargel, R, Haskin, J, Shani, V, Shainskaya, A, Manov, I, Liani, E, Avraham, E, Engelender, S

J. Biol. Chem. 2008
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Authored
Jupe, S  (2015-01-06)
Reviewed
Perry, G  (2015-11-09)
Created
Jupe, S  (2015-01-06)
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