Now showing items 1-3 of 3

    • Components of the Ubiquitin-Proteasome Pathway Compete for Surfaces on Rad23 Family Proteins 

      Goh, Amanda M; Walters, Kylie J; Elsasser, Suzanne; Verma, Rati; Deshaies, Raymond J; Finley, Daniel J.; Howley, Peter M. (BioMed Central, 2008)
      Background: The delivery of ubiquitinated proteins to the proteasome for degradation is a key step in the regulation of the ubiquitin-proteasome pathway, yet the mechanisms underlying this step are not understood in detail. ...
    • Rad23 escapes degradation because it lacks a proteasome initiation region 

      Fishbain, Susan; Prakash, Sumit; Herrig, Annie; Elsasser, Suzanne; Matouschek, Andreas (2014)
      Rad23 is an adaptor protein that binds to both ubiquitinated substrates and to the proteasome. Despite its association with the proteasome, Rad23 escapes degradation. Here we show that Rad23 remains stable because it lacks ...
    • USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites 

      Lee, Byung-Hoon; Lu, Ying; Prado, Miguel A.; Shi, Yuan; Tian, Geng; Sun, Shuangwu; Elsasser, Suzanne; Gygi, Steven P.; King, Randall W.; Finley, Daniel J. (Springer Nature, 2016)
      USP14 is a major regulator of the proteasome and one of three proteasome-associated deubiquitinating enzymes1-9. Its effects on protein turnover are substrate specific, for unknown reasons. We report that USP14 shows a ...