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CYLD: a deubiquitination enzyme with multiple roles in cancer.

Massoumi, Ramin LU (2011) In Future Oncology 7(2). p.285-297
Abstract
The post-translational modification of different proteins via direct ubiquitin attachment is important for various cellular processes. Dysregulation of components of the ubiqutin system have been linked to many diseases including cancer. CYLD is a deubiquitination enzyme that can cleave the lysine 63-linked polyubiquitin chains from target proteins and regulate cell survival or cell proliferation. Since loss of CYLD expression can be observed in different types of human cancer, it is now well established that CYLD acts as a tumor suppressor gene. Besides its loss of function in human tumors by gene deletion or mutation, CYLD expression can be downregulated at the RNA level if necessary through transcriptional regulation or at the protein... (More)
The post-translational modification of different proteins via direct ubiquitin attachment is important for various cellular processes. Dysregulation of components of the ubiqutin system have been linked to many diseases including cancer. CYLD is a deubiquitination enzyme that can cleave the lysine 63-linked polyubiquitin chains from target proteins and regulate cell survival or cell proliferation. Since loss of CYLD expression can be observed in different types of human cancer, it is now well established that CYLD acts as a tumor suppressor gene. Besides its loss of function in human tumors by gene deletion or mutation, CYLD expression can be downregulated at the RNA level if necessary through transcriptional regulation or at the protein level through post-translational modifications. This article summarizes recent advances that link CYLD to different types of human cancer. Identification of CYLD-mediated signaling pathways during the progression of cancer will provide a solid foundation for diagnosis and lead to the development of novel tools for cancer therapy. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Future Oncology
volume
7
issue
2
pages
285 - 297
publisher
Future Medicine Ltd.
external identifiers
  • wos:000288842100017
  • pmid:21345146
  • scopus:79952152655
ISSN
1479-6694
DOI
10.2217/fon.10.187
language
English
LU publication?
yes
id
5d80dd32-7214-478e-be8e-9de78d7f937f (old id 1831520)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/21345146?dopt=Abstract
date added to LUP
2011-03-01 17:43:07
date last changed
2017-10-29 04:30:32
@article{5d80dd32-7214-478e-be8e-9de78d7f937f,
  abstract     = {The post-translational modification of different proteins via direct ubiquitin attachment is important for various cellular processes. Dysregulation of components of the ubiqutin system have been linked to many diseases including cancer. CYLD is a deubiquitination enzyme that can cleave the lysine 63-linked polyubiquitin chains from target proteins and regulate cell survival or cell proliferation. Since loss of CYLD expression can be observed in different types of human cancer, it is now well established that CYLD acts as a tumor suppressor gene. Besides its loss of function in human tumors by gene deletion or mutation, CYLD expression can be downregulated at the RNA level if necessary through transcriptional regulation or at the protein level through post-translational modifications. This article summarizes recent advances that link CYLD to different types of human cancer. Identification of CYLD-mediated signaling pathways during the progression of cancer will provide a solid foundation for diagnosis and lead to the development of novel tools for cancer therapy.},
  author       = {Massoumi, Ramin},
  issn         = {1479-6694},
  language     = {eng},
  number       = {2},
  pages        = {285--297},
  publisher    = {Future Medicine Ltd.},
  series       = {Future Oncology},
  title        = {CYLD: a deubiquitination enzyme with multiple roles in cancer.},
  url          = {http://dx.doi.org/10.2217/fon.10.187},
  volume       = {7},
  year         = {2011},
}