| First Author | Zhang X | Year | 2004 |
| Journal | FEBS Lett | Volume | 559 |
| Issue | 1-3 | Pages | 57-60 |
| PubMed ID | 14960307 | Mgi Jnum | J:88977 |
| Mgi Id | MGI:3037530 | Doi | 10.1016/S0014-5793(04)00024-9 |
| Citation | Zhang X, et al. (2004) The mouse FKBP23 binds to BiP in ER and the binding of C-terminal domain is interrelated with Ca2+ concentration. FEBS Lett 559(1-3):57-60 |
| abstractText | FK506 binding protein 23 from mouse (mFKBP23) is a peptidyl-prolyl cis-trans isomerase (PPIase) from the endoplasmic reticulum (ER), which consists of an N-terminal PPIase domain and a C-terminal domain with Ca(2+) binding sites. The assay of adsorption from ER extract with glutathione S-transferase-mFKBP23 attached to glutathione-Sepharose 4B shows that mFKBP23 binds to mouse immunoglobulin binding protein (mBiP). The same assay with the recombinant proteins of the N- and C-termini of mFKBP23 shows that the binding of the C-terminus is Ca(2+)-dependent and the switch point is between 2 and 3 mM. By high concentration of Ca(2+) this binding cannot be detected. Furthermore, the Ca(2+)-regulated binding of mFKBP23 and mBiP in ER can be detected by means of co-immunoprecipitation. |
