CYLD in ubiquitin signaling and tumor pathogenesis

Cell. 2006 May 19;125(4):643-5. doi: 10.1016/j.cell.2006.05.003.

Abstract

Absence of CYLD, which encodes a deubiquitinating enzyme, causes an inherited disease characterized by benign skin tumors. In this issue of Cell, Massoumi et al. (2006) show that CYLD deubiquitinates the coactivator Bcl-3, thereby preventing its translocation into the nucleus, where it normally interacts with NF-kappaB and activates transcription of proliferation genes in response to growth signals.

Publication types

  • Comment

MeSH terms

  • B-Cell Lymphoma 3 Protein
  • Deubiquitinating Enzyme CYLD
  • Genes, Tumor Suppressor
  • Humans
  • NF-kappa B / metabolism
  • Neoplasms / metabolism*
  • Neoplasms / pathology
  • Proto-Oncogene Proteins / metabolism
  • Signal Transduction / physiology*
  • Transcription Factors
  • Tumor Suppressor Proteins / genetics
  • Tumor Suppressor Proteins / metabolism*
  • Ubiquitin / metabolism*

Substances

  • B-Cell Lymphoma 3 Protein
  • BCL3 protein, human
  • NF-kappa B
  • Proto-Oncogene Proteins
  • Transcription Factors
  • Tumor Suppressor Proteins
  • Ubiquitin
  • CYLD protein, human
  • Deubiquitinating Enzyme CYLD