CYLD in ubiquitin signaling and tumor pathogenesis.
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.
Ikeda
Fumiyo
F
Institute for Biochemistry II, Goethe University Medical School, Frankfurt 60590, Germany.
Dikic
Ivan
I
D000081242:B-Cell Lymphoma 3 Protein; D000074749:Deubiquitinating Enzyme CYLD; D016147:Genes, Tumor Suppressor; D006801:Humans; D016328:NF-kappa B / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D014157:Transcription Factors; D025521:Tumor Suppressor Proteins / Q000235:genetics / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*
D000081242:B-Cell Lymphoma 3 Protein; C000631344:BCL3 protein, human; D016328:NF-kappa B; D011518:Proto-Oncogene Proteins; D014157:Transcription Factors; D025521:Tumor Suppressor Proteins; D025801:Ubiquitin; C409984:CYLD protein, human; D000074749:Deubiquitinating Enzyme CYLD