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Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization.
Biochem Biophys Res Commun. 2011 May 20; 408(4):537-40.BB

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 [Ca(2+)]. 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.

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Authors+Show Affiliations

Feng M
Biochemical Section of Key Laboratory of Functional Polymer Materials, The Ministry of Education of China, Chemical School of Nankai University, Tianjin, PR China.
Gu C
No affiliation info available
Ma S
No affiliation info available
Wang Y
No affiliation info available
Liu H
No affiliation info available
Han R
No affiliation info available
Gao J
No affiliation info available
Long Y
No affiliation info available
Mi H
No affiliation info available

MeSH

AnimalsCalcium-Binding ProteinsCatalysisHeat-Shock ProteinsIsomerismLeucineMiceMolecular Sequence DataMutationPeptidylprolyl IsomeraseProlineProtein ConformationSubstrate SpecificityTacrolimus Binding Proteins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21527244

Citation

Feng, Miao, et al. "Mouse FKBP23 Mediates Conformer-specific Functions of BiP By Catalyzing Pro117 Cis/trans Isomerization." Biochemical and Biophysical Research Communications, vol. 408, no. 4, 2011, pp. 537-40.
Feng M, Gu C, Ma S, et al. Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization. Biochem Biophys Res Commun. 2011;408(4):537-40.
Feng, M., Gu, C., Ma, S., Wang, Y., Liu, H., Han, R., Gao, J., Long, Y., & Mi, H. (2011). Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization. Biochemical and Biophysical Research Communications, 408(4), 537-40. https://doi.org/10.1016/j.bbrc.2011.04.050
Feng M, et al. Mouse FKBP23 Mediates Conformer-specific Functions of BiP By Catalyzing Pro117 Cis/trans Isomerization. Biochem Biophys Res Commun. 2011 May 20;408(4):537-40. PubMed PMID: 21527244.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization. AU - Feng,Miao, AU - Gu,Chao, AU - Ma,Shikui, AU - Wang,Ying, AU - Liu,Huijuan, AU - Han,Ruifang, AU - Gao,Junfei, AU - Long,Yi, AU - Mi,Huaifeng, Y1 - 2011/04/19/ PY - 2011/04/01/received PY - 2011/04/09/accepted PY - 2011/4/30/entrez PY - 2011/4/30/pubmed PY - 2011/8/4/medline SP - 537 EP - 40 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 408 IS - 4 N2 - 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 [Ca(2+)]. 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. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/21527244/Mouse_FKBP23_mediates_conformer_specific_functions_of_BiP_by_catalyzing_Pro117_cis/trans_isomerization_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(11)00635-8 DB - PRIME DP - Unbound Medicine ER -