XIAP monoubiquinates TLE

Stable Identifier
R-HSA-3322429
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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XIAP has been shown to ubiquitinate all human isoforms of TLE in vitro, likely in the conserved Q domain. Ubiquitination does not appear to affect the stability, localization or tetramerization of TLE; rather ubiquitination affects the interaction with TCF/LEF. Ubiquitinated TLE3 is not able to bind TCF7L2 (TCF4) in vitro and addition of XIAP to TLE3-TCF7L2 complexes promotes the dissociation of TLE from TCF7L2. Although XIAP ubiquitinates TLE in a constitutive manner, XIAP only co-immunoprecipitates with TCF7L2 upon activation of the WNT signalling pathway. These data support a model where XIAP regulates the interaction between TLE and TCF/LEF by limiting the pool of free nuclear TLE that is available for binding, and by potentially disrupting existing repression complexes at WNT-responsive promoters. By disrupting the interaction between TLE and TCF/LEF, XIAP may facilitate the recruitment of beta-catenin and the establishment of an activation complex at WNT-responsive promoters (Hanson et al, 2012)
Literature References
PubMed ID Title Journal Year
22304967 XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling

Beauchamp, RD, Freeman, TJ, Wallace, HA, Hanson, AJ, Lee, E, Lee, LA

Mol. Cell 2012
Participants
Participates
Catalyst Activity

ubiquitin protein ligase activity of TLE:XIAP [nucleoplasm]

Orthologous Events
Authored
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