Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-3-16
pubmed:abstractText
KLF5 is a Kruppel-like zinc finger transcription factor modulating cell proliferation, differentiation, cell cycle, apoptosis, and angiogenesis. The KLF5 protein undergoes multiple posttranslational modifications including phosphorylation, acetylation and ubiquitination. We have demonstrated that the KLF5 protein can be ubiquitinated by the WWP1 E3 ubiquitin ligase and degraded by the proteasome. In this study, we found that KLF5 protein degradation is blocked by an N-terminal FLAG tag or a small N-terminal deletion without reducing ubiquitination and degradation mediated by WWP1. Interestingly, the N-terminal fragments of KLF5 containing the first 237 or 171 amino acids are as unstable as the full length KLF5 protein. The N-terminal FLAG tag or 19 amino acid deletion also delayed the degradation of the C-terminal truncated KLF5 proteins. To further understand the mechanism, we generated a lysine-less mutant KLF5(1-171). This mutant is efficiently degraded by the proteasome without ubiquitination in vitro and in vivo. These findings suggest that KLF5 protein degradation by the proteasome could be regulated in a ubiquitin-independent manner.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
581
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1124-30
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Proteasomal degradation of the KLF5 transcription factor through a ubiquitin-independent pathway.
pubmed:affiliation
The Center for Cell Biology and Cancer Research, MS355, Albany Medical College, 47 New Scotland Avenue, Albany, NY 12208, USA. chenc@mail.amc.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't