BRCA1 ubiquitylation of CtIP: Just the tIP of the iceberg?

DNA Repair (Amst). 2006 Dec 9;5(12):1499-504. doi: 10.1016/j.dnarep.2006.08.009. Epub 2006 Oct 5.

Abstract

Ubiquitylation is an important regulatory mechanism of many cellular processes. The breast and ovarian cancer-specific tumour suppressor BRCA1 is well acknowledged to be a RING/E3 ubiquitin ligase, however, identification of its physiological substrates has proved elusive. Recently published data have shown that the BRCA1-interacting protein CtIP is in fact ubiquitylated by BRCA1, and opens new avenues for the isolation of other substrate proteins.

MeSH terms

  • Animals
  • BRCA1 Protein / metabolism*
  • Carrier Proteins / metabolism*
  • Cell Cycle
  • DNA Repair*
  • Nuclear Proteins / metabolism*
  • Ubiquitin / metabolism*
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • BRCA1 Protein
  • Carrier Proteins
  • Nuclear Proteins
  • Ubiquitin
  • Ubiquitin-Protein Ligases