Linked Life Data

19204938

Source:http://linkedlifedata.com/resource/pubmed/id/19204938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-3-26
pubmed:abstractText
E6-associated protein (E6AP) is a cellular ubiquitin protein ligase that mediates ubiquitylation and degradation of p53 in conjunction with the high-risk human papillomavirus E6 proteins. However, the physiological functions of E6AP are poorly understood. To identify a novel biological function of E6AP, we screened for binding partners of E6AP using GST pull-down and mass spectrometry. Here we identified annexin A1, a member of the annexin superfamily, as an E6AP-binding protein. Ectopic expression of E6AP enhanced the degradation of annexin A1 in vivo. RNAi-mediated downregulation of endogenous E6AP increased the levels of endogenous annexin A1 protein. E6AP interacted with annexin A1 and induced its ubiquitylation in a Ca(2+)-dependent manner. GST pull-down assay revealed that the annexin repeat domain III of annexin A1 is important for the E6AP binding. Taken together, our data suggest that annexin A1 is a novel substrate for E6AP-mediated ubiquitylation. Our findings raise the possibility that E6AP may play a role in controlling the diverse functions of annexin A1 through the ubiquitin-proteasome pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1097-4644
pubmed:author
pubmed:copyrightInfo
Copyright 2009 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
106
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1123-35
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Identification of annexin A1 as a novel substrate for E6AP-mediated ubiquitylation.
pubmed:affiliation
Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't