Disordered Motifs and Domains in Cell Control - October 11-15, 2014

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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