Peroxisomes take shape
JJ Smith, JD Aitchison - Nature reviews Molecular cell biology, 2013 - nature.com
Peroxisomes carry out various oxidative reactions that are tightly regulated to adapt to the
changing needs of the cell and varying external environments. Accordingly, they are …
changing needs of the cell and varying external environments. Accordingly, they are …
[HTML][HTML] Multiple pathways for protein transport to peroxisomes
PK Kim, EH Hettema - Journal of molecular biology, 2015 - Elsevier
Peroxisomes are unique among the organelles of the endomembrane system. Unlike other
organelles that derive most if not all of their proteins from the ER (endoplasmic reticulum) …
organelles that derive most if not all of their proteins from the ER (endoplasmic reticulum) …
PEX5 translocation into and out of peroxisomes drives matrix protein import
ML Skowyra, TA Rapoport - Molecular cell, 2022 - cell.com
Peroxisomes are ubiquitous organelles whose dysfunction causes fatal human diseases.
Most peroxisomal enzymes are imported from the cytosol by the receptor PEX5, which …
Most peroxisomal enzymes are imported from the cytosol by the receptor PEX5, which …
The peroxisomal importomer constitutes a large and highly dynamic pore
M Meinecke, C Cizmowski, W Schliebs, V Krüger… - Nature cell …, 2010 - nature.com
The peroxisomal protein import machinery differs fundamentally from known translocons
(endoplasmic reticulum, mitochondria, chloroplasts, bacteria) as it allows membrane …
(endoplasmic reticulum, mitochondria, chloroplasts, bacteria) as it allows membrane …
Pex8p: an intraperoxisomal organizer of the peroxisomal import machinery
B Agne, NM Meindl, K Niederhoff, H Einwächter… - Molecular cell, 2003 - cell.com
Peroxisomes transport folded and oligomeric proteins across their membrane. Two cytosolic
import receptors, Pex5p and Pex7p, along with approximately 12 membrane-bound …
import receptors, Pex5p and Pex7p, along with approximately 12 membrane-bound …
The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol
V Dammai, S Subramani - Cell, 2001 - cell.com
Peroxisomal targeting signals (PTSs) are recognized by predominantly cytosolic receptors,
Pex5p and Pex7p. The fate of these PTS receptors following their interactions on the …
Pex5p and Pex7p. The fate of these PTS receptors following their interactions on the …
The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance
M Kunze, J Berger - Frontiers in physiology, 2015 - frontiersin.org
The proper distribution of proteins between the cytosol and various membrane-bound
compartments is crucial for the functionality of eukaryotic cells. This requires the cooperation …
compartments is crucial for the functionality of eukaryotic cells. This requires the cooperation …
Towards solving the mystery of peroxisomal matrix protein import
ML Skowyra, P Feng, TA Rapoport - Trends in Cell Biology, 2024 - cell.com
Peroxisomes are vital metabolic organelles that import their lumenal (matrix) enzymes from
the cytosol using mobile receptors. Surprisingly, the receptors can even import folded …
the cytosol using mobile receptors. Surprisingly, the receptors can even import folded …
Peroxisomal matrix protein import: the transient pore model
R Erdmann, W Schliebs - Nature Reviews Molecular Cell Biology, 2005 - nature.com
Peroxisomes import folded, even oligomeric, proteins, which distinguishes the peroxisomal
translocation machinery from the well-characterized translocons of other organelles. How …
translocation machinery from the well-characterized translocons of other organelles. How …
Peroxisome biogenesis disorders
S Weller, SJ Gould, D Valle - Annual review of genomics and …, 2003 - annualreviews.org
The peroxisome biogenesis disorders (PBDs) comprise 12 autosomal recessive
complementation groups (CGs). The multisystem clinical phenotype varies widely in severity …
complementation groups (CGs). The multisystem clinical phenotype varies widely in severity …