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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A.

Cyclophilin B is targeted to the secretory pathway via an endoplasmic reticulum signal sequence. We analyzed the localization and trafficking of endogenous and transfected cyclophilin B in mammalian cells. Cyclophilin B accumulates both in the endoplasmic reticulum and in complexes on the plasma membrane. The immunosuppressant cyclosporin A specifically mobilizes cyclophilin B from the endoplasmic reticulum, and promotes the secretion of cyclophilin B into the medium. We suggest that cyclosporin A competes with endogenous plasma membrane proteins for association with cyclophilin B in the secretory pathway. These findings argue in favor of a role for cyclophilin B as a chaperone to proteins destined for the plasma membrane, rather than solely as a proline isomerase functioning within the endoplasmic reticulum.[1]

References

  1. Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A. Price, E.R., Jin, M., Lim, D., Pati, S., Walsh, C.T., McKeon, F.D. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
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