Abstract
FKBP23 was found in mouse endoplasmic reticulum (ER) in 1998. It consists of an N-terminal peptidyl-prolyl cis/trans isomerase (PPIase) domain and a C-terminal domain with Ca2+ binding sites. Previously, we reported that FKBP23 specifically binds to BiP, the main protein of the molecular chaperone Hsp70 in ER lumen, and the binding is interrelated with the Ca2+ concentration. In this work we have found the existence of the complex FKBP23/BiP by separation of an ER extract using gel filtration chromatography (GFC), and that the existence of this complex is Ca2+-interrelated. This result further verified the Ca2+-interrelated binding of these two proteins in vivo.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Blotting, Western
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Calcium-Binding Proteins / isolation & purification
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Calcium-Binding Proteins / metabolism*
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Chromatography, Gel / methods
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Endoplasmic Reticulum / metabolism
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Endoplasmic Reticulum Chaperone BiP
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Heat-Shock Proteins / isolation & purification
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Heat-Shock Proteins / metabolism*
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Mice
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Molecular Chaperones / isolation & purification
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Molecular Chaperones / metabolism*
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Tacrolimus Binding Proteins / isolation & purification
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Tacrolimus Binding Proteins / metabolism*
Substances
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Calcium-Binding Proteins
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Endoplasmic Reticulum Chaperone BiP
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Fkbp7 protein, mouse
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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