FKBP8 (E6F3T) Rabbit mAb #18582

FKBP8, also known as FKBP38, is a member of the FK506-binding protein (FKBP) family that interacts with the immunosuppressive drug FK506 through a conserved peptidyl-prolyl cis-trans isomerase (PPIase) domain (1,2). In contrast to other FKBP family members, the PPIase activity of FKBP8 is dependent on Ca²⁺-signaling through a Ca²⁺-calmodulin binding domain (3). Loss of FKBP8 leads to defects in neural tube and eye development (4,5). FKBP family members generally function as molecular chaperones interacting with distinct proteins (2). FKBP8 is predominantly localized to the endoplasmic reticulum and the mitochondrial outer membrane and has been found to interact with proteins controlling apoptosis, including Bcl-2 and Bcl-xL (6). In addition, FKBP8 was found to promote autophagy through association with Beclin-1, a key component for activation of the VPS34 lipid kinase required for initiation of autophagy (7). FKBP8 also promotes autophagy by inhibiting mTOR, a kinase that plays a key role in cell growth (8). FKBP8 can also play a role in the clearance of damaged mitochondria through mitophagy. It contains an amino-terminal LC3-interacting region (LIR) motif that binds strongly to LC3A and recruits lipidated LC3A to damaged mitochondria to induce Parkin-independent mitophagy and promote mitochondrial fragmentation (9,10).