Author: Wilson, Van G.
Title: Sumoylation at the Host-Pathogen Interface Document date: 2012_4_5
ID: 1awau7hm_23
Snippet: In vitro the recruitment of the ubiquitin ligase causes enhanced ubiquitination of SAE1and in vivo a GAM1 mutant that cannot bind the cullins is unable to decrease SAE1/2 levels, implicating ubiquitin mediated proteasomal degradation as the mechanism by which the SUMO activating enzyme is reduced in the presence of GAM1. However, SAE2 is not directly ubiquitinated in the ligase complex, so the loss of SAE2 appears to be due to its destabilization.....
Document: In vitro the recruitment of the ubiquitin ligase causes enhanced ubiquitination of SAE1and in vivo a GAM1 mutant that cannot bind the cullins is unable to decrease SAE1/2 levels, implicating ubiquitin mediated proteasomal degradation as the mechanism by which the SUMO activating enzyme is reduced in the presence of GAM1. However, SAE2 is not directly ubiquitinated in the ligase complex, so the loss of SAE2 appears to be due to its destabilization when not in complex with SAE1. The net result of GAM1 action on SAE1 is dramatic reduction in levels of both SAE1 and SAE2 with the resultant cessation of de novo sumoylation. Sumoylation is generally associated with transcriptional repression [84] , so global loss of sumoylation should result in a much more transcriptionally robust cellular environment for the virus [85] .
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