FKBP8
FKBP8 (FKBP prolyl isomerase 8, also known as FKBP38 and FKBPr38) is a member of the immunophilin family that localises to mitochondria. It acts as a calmodulin- and calcium-dependent peptidyl-prolyl cis-trans isomerase and is linked to the regulation of apoptosis. Browse Assay Genie's current range of FKBP8 research reagents below, or read on for the biology behind the target.
FKBP8 is annotated as a constitutively inactive peptidyl-prolyl cis-trans isomerase (PPIase) that becomes active when bound to calmodulin and calcium. It appears to act as a chaperone for BCL2, targeting it to the mitochondria and modulating its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex is thought to interfere with the binding of BCL2 to its targets, so the active form of FKBP8 may help regulate apoptosis. FKBP8 has also been implicated in the inhibition of infection by influenza A viruses (IAV).
The FKBP8 gene encodes a member of the immunophilin protein family. Immunophilins contribute to immunoregulation and to basic cellular processes such as protein folding and trafficking. HGNC places the protein in both the tetratricopeptide repeat domain containing group and the FKBP prolyl isomerase family. UniProt records its subcellular location as the mitochondrion and the mitochondrial membrane. Researchers studying the FKBP8 protein often do so in the context of mitochondrial apoptosis signalling.
NCBI Gene notes that, unlike other family members, the encoded protein does not seem to have PPIase (rotamase) activity in its own right, which fits the UniProt description of an enzyme that is inactive until calmodulin and calcium are bound. The same summary suggests a role in neurons associated with memory function. The protein was formerly named FK506-binding protein 8 (38kD), which is the origin of the alias FKBP38. Mouse and rat both carry an orthologous Fkbp8 gene.
FKBP8 chaperones BCL2 to mitochondria and modulates its phosphorylation, making it relevant to studies of how BCL2 interactions and apoptosis are controlled.
FKBP8 PPIase activity depends on calmodulin and calcium binding, linking this immunophilin to calcium-regulated enzyme activation.
As a mitochondrial membrane protein, FKBP8 is a useful subject for work on protein targeting and trafficking to mitochondria.
FKBP8 has been linked to inhibition of influenza A virus infection and may act in neurons associated with memory function.
FKBP8 is a peptidyl-prolyl cis-trans isomerase that is constitutively inactive until it binds calmodulin and calcium. It appears to chaperone BCL2 to mitochondria and modulate its phosphorylation, so it may regulate apoptosis. It has also been implicated in inhibiting influenza A virus infection.
FKBP8 is also called FKBP38 and FKBPr38. Earlier names include FK506-binding protein 8 (38kD) and FK506 binding protein 8, 38kDa. HGNC now uses FKBP prolyl isomerase 8, and UniProt lists the protein as peptidyl-prolyl cis-trans isomerase FKBP8.
Yes. Both mouse and rat have an orthologous gene named Fkbp8, so the protein can be studied in common rodent models. Check the datasheet of any product for its validated reactivity before choosing a reagent for a particular species.
Other FKBP prolyl isomerase family members and immunophilins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q14318; product specifications from Assay Genie datasheets.