Tripartite motif-containing protein 71 (TRIM71)

Tripartite motif-containing protein 71 (TRIM71) is an E3 ubiquitin-protein ligase and RNA-binding protein characterized by an N-terminal RING domain (conferring E3 ligase activity) and a C-terminal NHL domain (mediating RNA binding). TRIM71 is a key post-transcriptional regulator of gene expression in embryonic stem cells and neural progenitors, functioning mainly by binding to and repressing transcripts with hairpin motifs in their 3′UTRs, either leading to target degradation or inhibiting translation. It also interacts with the microRNA (miRNA) machinery, contributing independently and synergistically with miRNAs to repress target gene expression like CDKN1A/p21, thereby promoting self-renewal, proliferation, and maintenance of undifferentiated cell states. Mutations in TRIM71 are causative of congenital hydrocephalus and may have broader implications in stem cell biology and oncogenesis.

Other names

LIN41Lin-41E3 ubiquitin-protein ligase TRIM71Protein lin-41 homologRING-type E3 ubiquitin transferase TRIM71HYC4HYDCC1abnormal cell lineage LIN-41homolog of C. elegans Lin-41

Facilitation of ubiquitin-mediated protein degradation (as E3 ligase); Post-transcriptional repression of mRNAs (including miRNA-dependent mechanisms); RNA hairpin recognition and direct silencing of mRNA targets