title: From cell death to viral replication: the diverse functions of the membrane-associated FKBP38.
abstract: FKBP38 is in many ways an exceptional member of the FK506-binding proteins. The calmodulin-regulated activity of FKBP38 for instance is unique within this protein family. The activated FKBP38 participates in apoptosis signaling by inhibiting the anti-apoptotic Bcl-2. Beyond this role in programmed cell death, FKBP38 seems to be involved in very different cellular processes that do not necessarily depend on the FKBP domain. These functions involve regulation of the kinase mTOR, regulation of neural tube formation, regulation of cellular hypoxia response, but also Hepatitis C virus replication. Pharmacological targeting of FKBP38 might therefore prove a successful strategy for intervention in different FKBP38-dependent processes, including programmed cell death in cancer or neurodegenerative diseases.
authors.affiliation: NIH, Surgical Neurology Branch, NINDS, Bethesda, MD 20892-3704, USA.
authors.forename: Frank
authors.initials: F
authors.lastname: Edlich
authors.forename: Christian
authors.initials: C
authors.lastname: Lücke
mesh_terms: D000818:Animals; D017209:Apoptosis; D002147:Calmodulin / Q000378:metabolism; D016503:Drug Delivery Systems; D016174:Hepacivirus / Q000502:physiology; D006801:Humans; D009369:Neoplasms / Q000188:drug therapy / Q000473:pathology; D019636:Neurodegenerative Diseases / Q000188:drug therapy / Q000503:physiopathology; D022021:Tacrolimus Binding Proteins / Q000378:metabolism*; D014779:Virus Replication
chemical_list: D002147:Calmodulin; C471205:FKBP8 protein, human; D022021:Tacrolimus Binding Proteins