Disordered Motifs and Domains in Cell Control
Poster Session I
21-POS
Board 21
E2 Ubiquitin-Conjugating Enzyme Interacts with Ubiquitin Receptor Rpn13
Leah Randles
, Kylie J. Walters.
National Cancer Institute, Frederick, MD, USA.
Regulated protein degradation by proteasome is essential and contributes to a large spectrum of
cellular events, including cell cycle progression, DNA repair, and signal transduction. Substrate
ubiquitination by a 3-step E1-E2-E3 enzymatic cascade can signal for proteolysis by proteasome,
which houses two ubiquitin receptors in its 19S regulatory particle, Rpn13 and S5a. Prior to
proteolysis, substrates are deubiquitinated and Rpn13 recognizes ubiquitin with an N-terminal
domain and deubiquitinating enzyme Uch37 with a C-terminal domain. We have found Rpn13
N-terminal domain to bind a disordered portion of an E2 ubiquitin-conjugating enzyme that
functions in cell cycle progression. This poster will present functional and physical
interrogations into this Rpn13/E2 interaction.
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