title: FKBP38-Bcl-2 interaction: a novel link to chemoresistance.
abstract: FKBP38, a noncanonical member of the immunosuppressive drug FK506 binding protein (FKBP) family members, possesses an inducible rotamase. FKBP38 interacts with several proteins and regulates multiple signaling pathways such as cell survival, apoptosis, proliferation, and metastasis. Deregulation of apoptosis is associated with chemoresistance and tumor relapse. The antiapoptotic protein Bcl-2 is a key player for increasing the apoptotic threshold in response to various cytotoxic drugs. The molecular interaction of Bcl-2 with FKBP38 potentiates the biological function of Bcl-2 and contributes to tumorigenesis and chemoresistance. Here, we discuss recent advances in the role of FKBP38 in connection with Bcl-2 and its possible link to chemotherapeutic resistance.
authors.affiliation: School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.
authors.forename: Bo-Hwa
authors.initials: BH
authors.lastname: Choi
authors.forename: Ho Sup
authors.initials: HS
authors.lastname: Yoon
mesh_terms: D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology; D019008:Drug Resistance, Neoplasm; D006801:Humans; D009364:Neoplasm Recurrence, Local; D009369:Neoplasms / Q000188:drug therapy / Q000473:pathology*; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000378:metabolism*; D015398:Signal Transduction; D022021:Tacrolimus Binding Proteins / Q000378:metabolism*
chemical_list: D000970:Antineoplastic Agents; C471205:FKBP8 protein, human; D019253:Proto-Oncogene Proteins c-bcl-2; D022021:Tacrolimus Binding Proteins