E3 ubiquitin ligases, such as SCFGrr1, are enzymes that add ubiquitin chains to proteins targeting them to the proteasome for degradation. Deubiquitinating enzymes (DUBs) can counteract this activity by removing ubiquitin chains and thus rescue proteins from degradation. Our goal was to develop genetic and biochemical screening approaches to identify DUB substrates, and thus learn more about DUBs that may contribute to human disease. Our data suggests that the yeast DUBs Ubp3 and Ubp12 affect the stability of the Grr1 targets Cln2, Cln3, and Gic2.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Stanley, Pamela Fay

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-010912-184218

Advisor

• Adams, David S.

Year

• 2012

Sponsor

• Jennifer Benanti

Date created

• 2012-01-09

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright