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Comment
. 2019 Aug 6;27(8):1185-1187.
doi: 10.1016/j.str.2019.07.009.

UBE2S Learns Self-Control

Tatyana Bodrug  1 , Nicholas G Brown  2
Affiliations
Comment

UBE2S Learns Self-Control

Tatyana Bodrug et al. Structure. .

Abstract

In this issue of Structure, Liess et al. (2019) demonstrate that the cell cycle regulator UBE2S shuts itself off through autoubiquitination at a conserved lysine residue. Since E2s are at the center of the ubiquitination cascade, this presents a possible regulatory mechanism in a multitude of cellular processes.

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Figures

Figure 1.
Figure 1.. Schematic of UBE2S self-inactivation mechanisms and implications.
(A) UBE2S can exist in Lys+5-in or Lys+5-out states. The Lys+5-in conformation brings Lys+5 (Lys100) in proximity to the active site Cys (Ccat, Cys95) for the intramolecular transfer of Ub. This mechanism is postulated to be conserved in potentially ~25% of all E2s. (B) UBE2S can transfer its donor Ub from an active, closed UBE2S~Ub to 1) Lys11 on a substrate-linked Ub to form chains on E3-bound substrates for proteasomal degradation; 2) Lys+5 inactivating UBE2S by blocking E1-mediated recharging of UBE2S-Ub with another donor Ub; or 3) lysines on the C-terminal peptide (CTP) extension of UBE2S marking itself for destruction.
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Comment on

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