TRIM-NHL as RNA Binding Ubiquitin E3 Ligase (RBUL): Implication in development and disease pathogenesis

Biochim Biophys Acta Mol Basis Dis. 2021 Jul 1;1867(7):166066. doi: 10.1016/j.bbadis.2020.166066. Epub 2021 Jan 6.

Abstract

TRIM proteins are RING domain-containing modular ubiquitin ligases, unique due to their stimuli specific expression, localization, and turnover. The TRIM family consists of more than 76 proteins, including the TRIM-NHL sub-family which possesses RNA binding ability along with the inherent E3 Ligase activity, hence can be classified as a unique class of RNA Binding Ubiquitin Ligases (RBULs). Having these two abilities, TRIM-NHL proteins can play important role in a wide variety of cellular processes and their dysregulation can lead to complex and systemic pathological conditions. Increasing evidence suggests that TRIM-NHL proteins regulate RNA at the transcriptional and post-transcriptional level having implications in differentiation, development, and many pathological conditions. This review explores the evolving role of TRIM-NHL proteins as TRIM-RBULs, their ubiquitin ligase and RNA binding ability regulating cellular processes, and their possible role in different pathophysiological conditions.

Keywords: E3 ubiquitin ligases; NHL domain; Neurodevelopment; Pathophysiology; RNA-binding proteins; miRNA regulation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Genetic Diseases, Inborn / metabolism
  • Genetic Diseases, Inborn / pathology*
  • Humans
  • RNA / metabolism*
  • RNA-Binding Proteins / metabolism*
  • Tripartite Motif Proteins / metabolism*
  • Ubiquitin
  • Ubiquitin-Protein Ligases / metabolism*
  • Ubiquitination

Substances

  • RNA-Binding Proteins
  • Tripartite Motif Proteins
  • Ubiquitin
  • RNA
  • Ubiquitin-Protein Ligases