Dual protein trafficking to secretory and non-secretory cell compartments clear or double vision?

Dual protein trafficking to secretory and non-secretory cell compartments : clear or double vision?

Copyright © 2015 Elsevier Ireland Ltd. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 234(2015) vom: 28. Mai, Seite 174-9
1. Verfasser: Porter, Brad W (VerfasserIn)
Weitere Verfasser: Yuen, Christen Y L, Christopher, David A
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Research Support, U.S. Gov't, Non-P.H.S. Review Co-translocation Dual targeting Protein disulfide isomerase Secretory pathway Signal peptide Signal recognition particle system Protein Sorting Signals mehr... Protein Disulfide-Isomerases EC 5.3.4.1
Beschreibung
Zusammenfassung:Copyright © 2015 Elsevier Ireland Ltd. All rights reserved.
Approximately 18% of Arabidopsis thaliana proteins encode a signal peptide for translocation to the endoplasmic reticulum (ER), the gateway of the eukaryotic secretory pathway. However, it was recently discovered that some ER proteins can undergo both co-translational import into the ER/secretory pathway and trafficking to compartments outside of the secretory pathway. This phenomenon is observed among members of the protein disulfide isomerase (PDI) family, which are traditionally regarded as ER enzymes involved in protein folding. Although classical PDIs possess an N-terminal signal peptide and a C-terminal ER retention signal, some also dual localize to secretory and non-secretory compartments, including mammalian PDI ERp57, Chlamydomonas reinhardtii PDI RB60, and A. thaliana AtPDI2. ERp57 is present in both the ER and nucleus where it influences gene transcription. RB60 localizes to the ER and chloroplast where it modulates the redox state of polyadenylate-binding protein RB47. AtPDI2, which interacts with transcription factor MEE8, localizes to the ER-secretory pathway and the nucleus. A model proposing secretory trafficking of AtPDI2 and nuclear co-translocation of an AtPDI2-MEE8 complex illustrates the diversity of dual targeting mechanisms, the multifunctional roles of some PDIs, and the potential co-translocation of other proteins to multiple subcellular compartments
Beschreibung:Date Completed 12.01.2016
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2259
DOI:10.1016/j.plantsci.2015.02.013