Characterization of estrogen-induced F-box protein FBXO45

Oncol Rep. 2005 Aug;14(2):531-5.

Abstract

Members of the F-box protein family are characterized by an approximately 40-amino-acid F-box domain. SCF complexes, formed by Skp1, Cullin, and F-box proteins, act as protein-ubiquitin ligases. F-box proteins interact with Skp1 through the F-box, and with ubiquitination targets. Therefore, F-box proteins are implicated in cell cycle regulation and signal transduction. We characterized the FBXO45 gene, a recently identified F-box protein, as an estrogen-induced gene. By using bioinformatics, human and mouse FBXO45 (286 aa) showed 100% total-amino-acid identity. Human and mouse FBXO45 genes consisting of 3 exons, and the vicinity of the transcriptional start site had several estrogen receptor binding consensus sequences. Finally, human FBXO45 mRNA was rapidly elevated by 17beta-estradiol in MCF-7 cells.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites / genetics
  • Cell Line, Tumor
  • Estradiol / pharmacology*
  • Exons
  • F-Box Proteins / genetics*
  • Gene Expression Regulation, Neoplastic / drug effects
  • Genes / genetics
  • Humans
  • Introns
  • Mice
  • Molecular Sequence Data
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Receptors, Estrogen / metabolism
  • Regulatory Sequences, Nucleic Acid / genetics
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • F-Box Proteins
  • FBXO45 protein, human
  • RNA, Messenger
  • Receptors, Estrogen
  • Estradiol