Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro(117) cis/trans isomerization

作者：Feng, Miao; Gu, Chao; Ma, Shikui; Wang, Ying; Liu, Huijuan; Han, Ruifang; Gao, Junfei; Long, Yi; Mi, Huaifeng^*

来源：Biochemical and Biophysical Research Communications, 2011, 408(4): 537-540.

DOI：10.1016/j.bbrc.2011.04.050

• Immunoglobulin binding protein
• Molecular switch
• FK506-binding protein
• Trigger factor

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 Pro(117) cis/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.

• 出版日期2011-5-20
• 单位南开大学