Differential loss of prolyl isomerase or chaperone activity of ran-binding protein 2 (Ranbp2) unveils distinct physiological roles of its cyclophilin domain in proteostasis


Journal Article

Background: Cyclophilins harbor ill-defined chaperone and prolyl isomerase activities toward physiological substrates. Results: Nonoverlapping chaperone or prolyl isomerase activity loss of Ran-binding protein 2 (Ranbp2) cyclophilin domain triggers unique impairments of proteostasis in distinct cell types and ubiquitin-proteasome system. Conclusion: Ranbp2 cyclophilin subdomains present discriminating physiological activities toward substrates or regulation of ubiquitin-proteasome system. Significance: Ranbp2-mediated mechanistic links in proteostasis with physiological and therapeutic relevance are uncovered. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

Full Text

Duke Authors

Cited Authors

  • Cho, KI; Patil, H; Senda, E; Wang, J; Yi, H; Qiu, S; Yoon, D; Yu, M; Orry, A; Peachey, NS; Ferreira, PA

Published Date

  • February 21, 2014

Published In

Volume / Issue

  • 289 / 8

Start / End Page

  • 4600 - 4625

Electronic International Standard Serial Number (EISSN)

  • 1083-351X

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M113.538215

Citation Source

  • Scopus