Ub-SNCA dissociates from the conjugating enzyme

Stable Identifier
Reaction [uncertain]
Homo sapiens
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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
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
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
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