Efp/TRIM25 and Its Related Protein, TRIM47, in Hormone-Dependent Cancers

Cells. 2022 Aug 8;11(15):2464. doi: 10.3390/cells11152464.

Abstract

Increasing attention has been paid to the biological roles of tripartite motif-containing (TRIM) family proteins, which typically function as E3 ubiquitin ligases. Estrogen-responsive finger protein (Efp), a member of the TRIM family proteins, also known as TRIM25, was originally identified as a protein induced by estrogen and plays critical roles in promoting endocrine-related cancers, including breast cancer, endometrial cancer, and prostate cancer. The pathophysiological importance of Efp made us interested in the roles of other TRIM family proteins that share a similar structure with Efp. Based on a phylogenetic analysis of the C-terminal region of TRIM family proteins, we focused on TRIM47 as a protein belonging to the same branch as Efp. TRIM47 is a poor prognostic factor in both breast cancer and prostate cancer. Atypical lysine-27-like poly-ubiquitination was involved in the underlying mechanism causing endocrine resistance in breast cancer. We also discuss the functions of Efp and TRIM47 in other types of cancers and innate immunity by introducing substrates the are modified by poly-ubiquitination.

Keywords: TRIM family proteins; TRIM25; TRIM47; breast cancer; endometrial cancer; estrogen-responsive finger protein (Efp); hormone-dependent cancers; prostate cancer.

Publication types

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

MeSH terms

  • Breast / metabolism
  • Breast Neoplasms* / genetics
  • Breast Neoplasms* / metabolism
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Estrogens
  • Humans
  • Male
  • Neoplasm Proteins / metabolism
  • Nuclear Proteins / metabolism
  • Phylogeny
  • Prostatic Neoplasms* / genetics
  • Prostatic Neoplasms* / metabolism
  • Transcription Factors / metabolism
  • Tripartite Motif Proteins / genetics
  • Tripartite Motif Proteins / metabolism
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • Carrier Proteins
  • Estrogens
  • Neoplasm Proteins
  • Nuclear Proteins
  • TRIM47 protein, human
  • Transcription Factors
  • Tripartite Motif Proteins
  • TRIM25 protein, human
  • Ubiquitin-Protein Ligases

Grants and funding

This study was supported by grants from the Cell Innovation Program (S.I.), P-DIRECT (S.I.) and P-CREATE (S.I.) from the Ministry of Education, Culture, Sports, Science, and Technology (MEXT), Japan; by Grants-in-Aid for S.I. (15K15353), and K.A. (17K10571 and 20K08954) from the Japan Society for the Promotion of Science (JSPS), Japan; by a grant from Uehara Memorial Foundation (S.I.); by a grant from Yamaguchi Endocrine Research Foundation (K.A.); and by a grant from Kao Health Science Foundation (K.A.).