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. 1994 Apr 26;91(9):3931–3935. doi: 10.1073/pnas.91.9.3931

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

E R Price 1, M Jin 1, D Lim 1, S Pati 1, C T Walsh 1, F D McKeon 1
PMCID: PMC43696  PMID: 7909608

Abstract

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.

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Selected References

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