Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Procis/trans isomerization |
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| Authors: | Miao Feng Chao Gu Shikui Ma Ying Wang Huijuan Liu Ruifang Han Junfei Gao Yi Long Huaifeng Mi |
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| Institution: | Biochemical Section of Key Laboratory of Functional Polymer Materials, The Ministry of Education of China, Chemical School of Nankai University, 300071 Tianjin, PR China |
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| Abstract: | FK506-binding proteins (FKBPs) are cellular receptors for the immunosuppressant FK506 and rapamycin. They belong to the ubiquitous peptidyl-prolyl cis/trans isomerases (PPIases) family, which can catalyze the cis/trans isomerization of peptidyl-prolyl bond in peptides and proteins. In previous work, we revealed that mouse FKBP23 binds immunoglobulin binding protein (BiP), the major heat shock protein (Hsp) 70 chaperone in the ER, and the binding is interrelated with Ca2+]. Furthermore, the binding can suppress the ATPase activity of BiP through the PPIase activity of FKBP23. In this work, FKBP23 is demonstrated to mediate functions of BiP by catalyzing the Pro117cis/trans conformational interconversion in the ATPase domain of BiP. This result may provide new understanding to the novel role of PPIase as a molecular switch. |
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| Keywords: | Abbreviations: mBiP mouse immunoglobulin binding protein ER endoplasmic reticulum CyPs cyclophilins mFKBP mouse FK506-binding protein PPIase peptidyl-prolyl cis/trans isomerase Hsp heat shock protein mFKBP23N N-terminus of mFKBP23 mBiPN N-terminus of mBiP Suc succinyl pNA p-nitroanilide WT wild-type |
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