Alternative and aberrant splicing of MDM2 mRNA in human cancer.
MDM2 has been characterized as a protein that binds to and facilitates degradation of the tumor suppressor p53. Interestingly, more than 40 different splice variants of MDM2 transcripts have been identified both in tumors and normal tissues, and the majority of these variants do not contain sequence encoding the p53 binding site. This review describes the different splice forms, the tissues in which they have been identified, and their association with tumor progression and prognosis. In addition, we discuss the potential functions of these variants and how they interact with full-length MDM2 protein.
Bartel
Frank
F
Department of Molecular Pharmacology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
Taubert
Helge
H
Harris
Linda C
LC
D017398:Alternative Splicing; D000818:Animals; D001665:Binding Sites; D006801:Humans; D008957:Models, Genetic; D009154:Mutation; D009363:Neoplasm Proteins / Q000235:genetics; D009369:Neoplasms / Q000235:genetics* / Q000473:pathology; D009687:Nuclear Proteins; D011379:Prognosis; D020033:Protein Isoforms / Q000235:genetics* / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D051736:Proto-Oncogene Proteins c-mdm2; D012333:RNA, Messenger / Q000235:genetics* / Q000378:metabolism; D014407:Tumor Cells, Cultured; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism
D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D020033:Protein Isoforms; D011518:Proto-Oncogene Proteins; D012333:RNA, Messenger; D016159:Tumor Suppressor Protein p53; C497206:MDM2 protein, human; D051736:Proto-Oncogene Proteins c-mdm2