PuSH - Publication Server of Helmholtz Zentrum München

Emmanouilidis, L. ; Gopalswamy, M. ; Passon, D.M.* ; Wilmanns, M.* ; Sattler, M.

Structural biology of the import pathways of peroxisomal matrix proteins.

Biochim. Biophys. Acta-Mol. Cell Res. 1863, 804-813 (2016)
Publ. Version/Full Text DOI PMC
Closed
Open Access Green as soon as Postprint is submitted to ZB.
The peroxisomal proteins (peroxins) that mediate the import of peroxisomal matrix proteins have been identified. Recently, the purification of a functional peroxisomal translocon has been reported. However, the molecular details of the import pathways and the mechanisms by which the cargo is translocated into the lumen of the organelle are still poorly understood. Structural studies have begun to provide insight into molecular mechanisms of peroxisomal import pathways for cargo proteins that harbor peroxisomal targeting signals, PTS1 and PTS2, at their C- and N-termini, respectively. So far structures have been reported for binary or tertiary protein-protein interfaces, and highlight the role of intrinsically disordered regions for these interactions. Here, we provide an overview of the currently available structural biology of peroxisomal import pathways. Current challenges and future perspectives of the structural biology of peroxisomal protein translocation are discussed.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Scopus
Cited By
Altmetric
5.128
1.311
24
28
Tags
Annotations
Special Publikation
Hide on homepage

Edit extra information
Edit own tags
Private
Edit own annotation
Private
Hide on publication lists
on hompage
Mark as special
publikation
Publication type Article: Journal article
Document type Scientific Article
Keywords Peroxisomal Matrix Proteins ; Peroxisomal Translocon ; Peroxisome Biogenesis ; Pex13 ; Pex14 ; Pex5 ; Pex7 ; Pts1 ; Pts2 ; Structural Biology; Targeting Signal Receptor; N-terminal Domain; Cerebrohepatorenal Zellweger Syndrome; Complete Dna-sequence; Ovary Cell Mutant; Acyl-coa Oxidase; Saccharomyces-cerevisiae; Pts1 Receptor; Membrane-protein; Crystal-structure
Language english
Publication Year 2016
Prepublished in Year 2015
HGF-reported in Year 2015
ISSN (print) / ISBN 0167-4889
e-ISSN 1879-2596
Quellenangaben Volume: 1863, Issue: 5, Pages: 804-813 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place Amsterdam
Reviewing status Peer reviewed
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503000-001
Scopus ID 84961180169
Scopus ID 84951325688
PubMed ID 26450166
Erfassungsdatum 2015-12-09