Post-translational regulation of COX2 activity by FYN in prostate cancer cells. Oncotarget 2014 Jun 30;5(12):4232-43
Date
06/28/2014Pubmed ID
24970799Pubmed Central ID
PMC4147319DOI
10.18632/oncotarget.1983Scopus ID
2-s2.0-84905119291 (requires institutional sign-in at Scopus site) 22 CitationsAbstract
While increased COX2 expression and prostaglandin levels are elevated in human cancers, the mechanisms of COX2 regulation at the post-translational level are unknown. Initial observation that COX2 forms adduct with non-receptor tyrosine kinase FYN, prompted us to study FYN-mediated post-translational regulation of COX2. We found that FYN increased COX2 activity in prostate cancer cells DU145, independent of changes in COX2 or COX1 protein expression levels. We report that FYN phosphorylates human COX2 on Tyr 446, and while corresponding phospho-mimetic COX2 mutation promotes COX2 activity, the phosphorylation blocking mutation prevents FYN-mediated increase in COX2 activity.
Author List
Alexanian A, Miller B, Chesnik M, Mirza S, Sorokin AAuthor
Andrey Sorokin PhD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Cyclooxygenase 2Humans
Male
Membrane Proteins
Phosphorylation
Prostatic Neoplasms
Protein Processing, Post-Translational
Proto-Oncogene Proteins c-fyn
Transfection