Identification of Tropoelastin as a Ligand for the 65-kD FK506-binding Protein, FKBP65, in the Secretory Pathway

doi:10.1083/jcb.140.2.295

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J. Cell Biol., Volume 140, Number 2, January 26, 1998 295-303

Identification of Tropoelastin as a Ligand for the 65-kD FK506-binding Protein, FKBP65, in the Secretory Pathway

Elaine C. Davis,^* Thomas J. Broekelmann,^* Yuji Ozawa,^* and Robert P. Mecham^*

^* Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110 and Respiratory and Critical Care Division, Department of Medicine, Barnes-Jewish Hospital, St. Louis, Missouri 63110

The folding and trafficking of tropoelastin is thought to be mediated by intracellular chaperones, although the identity androle of any tropoelastin chaperone remain to be determined. Toidentify proteins that are associated with tropoelastin intracellularly,bifunctional chemical cross-linkers were used to covalently stabilizeinteractions between tropoelastin and associated proteins in thesecretory pathway in intact fetal bovine auricular chondrocytes.Immunoprecipitation of tropoelastin from cell lysates after cross-linkingand analysis by SDS-PAGE showed the presence of two proteins of~74 kD (p74) and 78 kD (p78) that coimmunoprecipitated with tropoelastin.Microsequencing of peptide fragments from a cyanogen bromide digestof p78 identified this protein as BiP and sequence analysis identifiedp74 as the peptidyl-prolyl cis-trans isomerase, FKPB65. The appearanceof BiP and FKBP65 in the immunoprecipitations could be enhancedby the addition of brefeldin A (BFA) and N-acetyl-leu-leu-norleucinal(ALLN) to the culture medium for the final 4 h of labeling. Tropoelastinaccumulates in the fused ER/Golgi compartment in the presenceof BFA if its degradation is inhibited by ALLN (Davis, E.C., andR.P. Mecham. 1996. J. Biol. Chem. 271:3787-3794). The use of BFAand other secretion-disrupting agents suggests that the associationof tropoelastin with FKBP65 occurs in the ER. Results from thisstudy provide the first identification of a ligand for an FKBPin the secretory pathway and suggest that the prolyl cis-transisomerase activity of FKBP65 may be important for the proper foldingof the proline-rich tropoelastin molecule before secretion.

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