Emerging roles of Lys63-linked polyubiquitylation in immune responses

Immunol Rev. 2015 Jul;266(1):161-74. doi: 10.1111/imr.12310.

Abstract

Among all the E2 ubiquitin-conjugating enzymes, Ubc13, which heterodimerizes with Uev1a, specifically mediates lysine 63 (K63)-linked protein polyubiquitylation, a process that does not lead to proteasomal degradation of its substrates. Instead, it plays a key role in signal transduction. Numerous roles of Lys63-linked polyubiquitylation in immune responses have emerged, indicating the importance of this regulatory strategy. Here, we summarize some of the signaling pathways that depend on Lys63-linked polyubiquitylation during innate and adaptive immune responses, with a focus on the underlying molecular mechanisms. In addition, we describe how Ubc13 itself is regulated and outline its function in transforming growth factor β signaling. We discuss the current progress in pharmacological targeting of Ubc13 in inflammatory and autoimmune diseases as well as cancer therapy.

Keywords: K63-polyubiquitylation; Ubc13; adaptive immunity; innate immunity.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptive Immunity
  • Animals
  • Humans
  • Immunity, Innate
  • Lysine / metabolism*
  • Signal Transduction
  • Transcription Factors / metabolism*
  • Transforming Growth Factor beta1 / metabolism
  • Ubiquitin-Conjugating Enzymes / metabolism*
  • Ubiquitination*

Substances

  • Transcription Factors
  • Transforming Growth Factor beta1
  • UBE2N protein, human
  • UBE2V1 protein, human
  • Ubiquitin-Conjugating Enzymes
  • Lysine