Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 1 to 3 of 3

Publication Record


Dynamics of the peroxisomal import cycle of PpPex20p: ubiquitin-dependent localization and regulation.
Léon S, Zhang L, McDonald WH, Yates J, Cregg JM, Subramani S
(2006) J Cell Biol 172: 67-78
MeSH Terms: Cytosol, Endocytosis, Fungal Proteins, Gene Deletion, Models, Molecular, Peroxisomal Targeting Signal 2 Receptor, Peroxisomes, Pichia, Receptors, Cytoplasmic and Nuclear, Signal Transduction, Ubiquitin
Show Abstract · Added March 20, 2014
We characterize the peroxin PpPex20p from Pichia pastoris and show its requirement for translocation of PTS2 cargoes into peroxisomes. PpPex20p docks at the peroxisomal membrane and translocates into peroxisomes. Its peroxisomal localization requires the docking peroxin Pex14p but not the peroxins Pex2p, Pex10p, and Pex12p, whose absence causes peroxisomal accumulation of Pex20p. Similarities between Pex5p and Pex20p were noted in their protein interactions and dynamics during import, and both contain a conserved NH2-terminal domain. In the absence of the E2-like Pex4p or the AAA proteins Pex1p and Pex6p, Pex20p is degraded via polyubiquitylation of residue K19, and the K19R mutation causes accumulation of Pex20p in peroxisome remnants. Finally, either interference with K48-branched polyubiquitylation or removal of the conserved NH2-terminal domain causes accumulation of Pex20p in peroxisomes, mimicking a defect in its recycling to the cytosol. Our data are consistent with a model in which Pex20p enters peroxisomes and recycles back to the cytosol in an ubiquitin-dependent manner.
0 Communities
1 Members
0 Resources
11 MeSH Terms
How are peroxisomes formed? The role of the endoplasmic reticulum and peroxins.
Mullen RT, Flynn CR, Trelease RN
(2001) Trends Plant Sci 6: 256-61
MeSH Terms: Ascorbate Peroxidases, Biological Transport, Endoplasmic Reticulum, Genes, Plant, Membrane Proteins, Models, Biological, Peroxidases, Peroxisomal Targeting Signal 2 Receptor, Peroxisome-Targeting Signal 1 Receptor, Peroxisomes, Plant Proteins, Plants, Receptors, Cytoplasmic and Nuclear, Sequence Homology, Signal Transduction, Yeasts
Show Abstract · Added December 10, 2013
Recent data from studies of peroxisome assembly and the subcellular sorting of peroxisomal matrix and membrane proteins have led to an expansion of the 'growth and division' and 'endoplasmic reticulum-vesiculation' models of peroxisome biogenesis into a more flexible, unified model. Within this context, we discuss the proposed role for the endoplasmic reticulum in the formation of preperoxisomes and the potential for 15 Arabidopsis peroxin homologs to function in the biogenesis of peroxisomes in plant cells.
0 Communities
1 Members
0 Resources
16 MeSH Terms
Mutational analyses of a type 2 peroxisomal targeting signal that is capable of directing oligomeric protein import into tobacco BY-2 glyoxysomes.
Flynn CR, Mullen RT, Trelease RN
(1998) Plant J 16: 709-20
MeSH Terms: Acetyl-CoA C-Acetyltransferase, Amino Acid Sequence, Animals, Cells, Cultured, Chloramphenicol O-Acetyltransferase, Conserved Sequence, Humans, Liver, Molecular Sequence Data, Organelles, Peroxisomal Targeting Signal 2 Receptor, Plants, Toxic, Rats, Receptors, Cytoplasmic and Nuclear, Recombinant Fusion Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Tobacco
Show Abstract · Added December 10, 2013
In this study of the type 2 peroxisomal targeting signal (PTS2) pathway, we examined the apparent discontinuity and conservation of residues within the PTS2 nonapeptide and demonstrated that this topogenic signal is capable of directing heteromultimeric protein import in plant cells. Based on cumulative data showing that at least 26 unique, putative PTS2 nonapeptides occur within 12 diverse peroxisomal-destined proteins, the current (-R/K-L/V/I-X5-H/Q-L/A-) as well as the original (-R-L-X5-H/Q-L-) PTS2 motif appear to be oversimplified. To assess the functionality of residues within the motif, rat liver thiolase (rthio) and various chimeric chloramphenicol acetyltransferase (CAT) proteins were expressed transiently in suspension-cultured tobacco (Nicotiana tabaccum L.) cv Bright Yellow cells (BY-2), and their subcellular location was determined by immunofluoresence microscopy. Hemagglutinin (HA)-epitope-tagged-CAT subunits, lacking a PTS2 (CAT-HA), were 'piggybacked' into glyoxysomes by PTS2-bearing CAT subunits (rthio-CAT), whereas signal-depleted CAT-HA subunits that were modified to prevent oligomerization did not import into glyoxysomes. These results provided direct evidence that signal-depleted subunits imported into peroxisomes were targeted to the organelle as oligomers (heteromers) by a PTS2. Mutational analysis of residues within PTS2 nonapeptides revealed that a number of amino acid substitutions were capable of maintaining targeting function. Furthermore, functionality of residues within the PTS2 nonapeptide did not appear to require a context-specific environment conferred by adjacent residues. These results collectively suggest that the functional PTS2 is not solely defined as a sequence-specific motif, i.e. -R/K-X6-H/Q-A/L/F-, but defined also by its structural motif that is dependent upon the physiochemical properties of residues within the nonapeptide.
0 Communities
1 Members
0 Resources
18 MeSH Terms