The binding of FKBP23 to BiP modulates BiP’s ATPase activity with its PPIase activity
Copyright policy )The binding of FKBP23 to BiP modulates BiP’s ATPase activity with its PPIase activity
Peptidyl-prolyl cis-trans-isomerases (PPIases) are enzymes that can cis-trans-isomerize a Xaa-Pro peptide bond. Three families of PPIases are known: cyclophilins, FKBPs, and parvulins. The physiological functions of the PPIases are only poorly understood. In previous work, we reported that the mouse FK506-binding protein 23 (mFKBP23), which comprises an N-terminal PPIase domain and a C-terminal domain with Ca(2+)-binding sites, binds to mBiP in the endoplasmic reticulum (ER) and this binding is affected by the Ca(2+) concentration. In this study, we demonstrate the ability of mFKBP23 to modulate the ATPase activity of BiP, and that the bound mFKBP23, but not the free mFKBP23, can suppress the ATPase activity of mBiP through its PPIase activity.
- Nankai University China (People's Republic of)
Adenosine Triphosphatases, Coenzymes, Peptidylprolyl Isomerase, Endoplasmic Reticulum, Enzyme Activation, Tacrolimus Binding Proteins, Mice, Hepatocytes, Animals, Endoplasmic Reticulum Chaperone BiP, Heat-Shock Proteins, Molecular Chaperones, Protein Binding
Adenosine Triphosphatases, Coenzymes, Peptidylprolyl Isomerase, Endoplasmic Reticulum, Enzyme Activation, Tacrolimus Binding Proteins, Mice, Hepatocytes, Animals, Endoplasmic Reticulum Chaperone BiP, Heat-Shock Proteins, Molecular Chaperones, Protein Binding
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