Translocator protein (18kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function.

  title={Translocator protein (18kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function.},
  author={Vassilios Papadopoulos and Mario Baraldi and Tom{\'a}s R. Guilarte and Thomas B. Knudsen and Jean‐Jacques Lacapere and Peter Lindemann and M D Norenberg and David J. Nutt and Abraham Weizman and Ming-Rong Zhang and Moshe Gavish},
  journal={Trends in pharmacological sciences},
  volume={27 8},
Channel-like functions of the 18-kDa translocator protein (TSPO): regulation of apoptosis and steroidogenesis as part of the host-defense response.
It is suggested that the involvement of TSPO and its ligands in such seemingly disparate biological functions as immunological responses, apoptosis, and steroidogenesis may have a common denominator in the multi-dimensional role of T SPO in the host-defense response to disease and injury.
Translocator protein (18 kDa): an update on its function in steroidogenesis
Taken together, these studies suggest that TSPO is a unique mitochondrial pharmacological target for diseases that involve increased mitochondrial activity, including steroidogenesis.
The mitochondrial translocator protein (TSPO): a key multifunctional molecule in the nervous system.
Translocator protein (TSPO, 18 kDa), formerly known as peripheral benzodiazepine receptor, is an evolutionary well-conserved protein located on the outer mitochondrial membrane. TSPO is involved in a
Translocator Protein 18 kDa (TSPO): An Old Protein with New Functions?
It is suggested that TSPO is an ancient bacterial receptor/stress sensor that has developed additional interactions, partners, and roles in its mitochondrial outer membrane environment in eukaryotes.
Regulation of translocator protein 18kDa (TSPO) expression in health and disease states
VDAC activation by the 18 kDa translocator protein (TSPO), implications for apoptosis
Understanding is provided regarding the mechanisms whereby VDAC and TSPO may serve as targets to modulate apoptotic rates, which has implications for drug design to treat diseases such as neurodegeneration and cancer.


A novel Arabidopsis thaliana protein is a functional peripheral-type benzodiazepine receptor.
Results suggest that the PBR like protein is involved in steroid import and is directing protoporphyrinogen IX to the mitochondrial site of protoheme formation.
Characterization of the cholesterol recognition amino acid consensus sequence of the peripheral-type benzodiazepine receptor.
Structural and functional evidence is provided supporting the finding that the CRAC domain in the cytosolic carboxyl-terminal domain of PBR might be responsible for the uptake and translocation of cholesterol into the mitochondria.
Peripheral-type benzodiazepine receptor-mediated action of steroidogenic acute regulatory protein on cholesterol entry into leydig cell mitochondria.
Reincorporation of in vitro transcribed/translated PBR, but not PBR missing the cholesterol-binding domain, into MA-10 mitochondria rescued the ability of the mitochondria to form steroids and the ability to respond to StAR and Tom/StAR proteins.
The peripheral‐type benzodiazepine receptor: a protein of mitochondrial outer membranes utilizing porphyrins as endogenous ligands
  • S. Snyder, A. Verma, R. Trifiletti
  • Biology, Chemistry
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1987
Interactions of porphyrins with the mitochondrial receptor may clarify its physiological role and account for many pharmacological actions of benzodiazepines.
Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier.
The mitochondrial benzodiazepine receptor has been solubilized with retention of reversible ligand binding, and the associated subunits were characterized, finding that VDAC and ADC, outer and inner mitochondrial membrane channel proteins, respectively, together with the 18-kDa subunit, may comprise mBzR at functionally important transport sites at the junction of two mitochondrial membranes.
In vitro reconstitution of a functional peripheral-type benzodiazepine receptor from mouse Leydig tumor cells.
Results provide strong evidence that PBR is not a single protein receptor but a multimeric complex in which the IQ binding site is on the M(r) 18,000 subunit and expression of the BZ binding site requires both the M (r) 24,000 and 34,000 voltage-dependent anion channel subunits.
Cholesterol binding at the cholesterol recognition/ interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide.
Results show that TAT-CRAC binds cholesterol and competes for cholesterol interaction with endogenous PBR, suggesting that the cytosolic carboxyl-terminal domain of PBR is responsible for taking up and bringing steroidogenic cholesterol into the mitochondria.