Linked Life Data

17577629

Source:http://linkedlifedata.com/resource/pubmed/id/17577629

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2007-10-2
pubmed:abstractText
Serine/threonine kinase Akt (also called protein kinase B, PKB) is a downstream effector of phosphoinositide 3-kinase (PI3K) and functions as the focal point for many signal transduction pathways such as glucose metabolism, transcription, cell survival, angiogenesis, and cell motility. Akt is emerging as a central player in tumorigenesis including human ovarian, pancreatic, prostate, breast, and gastric cancers. However, the function and mechanism by which Akt regulate gene transcription in nucleus remains largely unclear. Here we identify histone methyltransferase SETDB1 as a novel nuclear interacting partner of Akt. By yeast two-hybrid screening, we obtained the Akt1-SETDB1 interaction and confirmed the binding both in vitro and in vivo. Both Akt1 and SETDB1 are co-localized in the nucleus in mammalian cells. SETDB1 is not a phosphorylation substrate of Akt kinase. Akt and SETDB1 could coordinate to regulate the activity of certain transcription factors such as forkhead family member. Due to the fact that SETDB1 acts as a specific histone H3, lysine 9-methyltransferase in vivo, we provide the first link between Akt kinase and histone methyltransferase (HMTase). This interaction represents a novel mechanism by which Akt regulates nuclear events including gene transcription.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:volume
305
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35-44
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Akt/PKB interacts with the histone H3 methyltransferase SETDB1 and coordinates to silence gene expression.
pubmed:affiliation
Department of Breast Surgery, Qilu Hospital of Shandong University, Jinan, 250012, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't