Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Calcium / pharmacology*
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Calcium-Binding Proteins / metabolism*
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Carrier Proteins / metabolism*
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Endoplasmic Reticulum / metabolism*
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Endoplasmic Reticulum Chaperone BiP
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HSP70 Heat-Shock Proteins / metabolism
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Heat-Shock Proteins*
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Mice
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Molecular Chaperones / metabolism*
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Peptidylprolyl Isomerase / metabolism
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Protein Binding / drug effects
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Protein Structure, Tertiary
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Tacrolimus Binding Proteins / metabolism*
Substances
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Calcium-Binding Proteins
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Carrier Proteins
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Endoplasmic Reticulum Chaperone BiP
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Fkbp7 protein, mouse
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HSP70 Heat-Shock Proteins
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Heat-Shock Proteins
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Molecular Chaperones
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Recombinant Proteins
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Tacrolimus Binding Proteins
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Peptidylprolyl Isomerase
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Calcium