ArticleThe Journal of biological chemistry2009
Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Structure of Trypanosoma peroxisomal import complex unveils conformational heterogeneity.Nature communications · 2025Article
- Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis.Cells · 2022Review
- Diffusion and interaction dynamics of the cytosolic peroxisomal import receptor PEX5.Biophysical reports · 2022Article
- Studying the interaction between PEX5 and its full-length cargo proteins in living cells by a novel Försteŕs resonance energy transfer-based competition assay.Frontiers in cell and developmental biology · 2022Article
- Chemically monoubiquitinated PEX5 binds to the components of the peroxisomal docking and export machinery.Scientific reports · 2018Article
- Peroxisome protein import: a complex journey.Biochemical Society transactions · 2016Review
- Covalent Label Transfer between Peroxisomal Importomer Components Reveals Export-driven Import Interactions.The Journal of biological chemistry · 2016Article
- PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor.FEBS letters · 2014Article
- A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes.The Journal of biological chemistry · 2014Article
- PEX5 and ubiquitin dynamics on mammalian peroxisome membranes.PLoS computational biology · 2014Article
- A cargo-centered perspective on the PEX5 receptor-mediated peroxisomal protein import pathway.The Journal of biological chemistry · 2013Article
- Import of proteins into the peroxisomal matrix.Frontiers in physiology · 2013Review
- The exportomer: the peroxisomal receptor export machinery.Cellular and molecular life sciences : CMLS · 2013Review
- Lipid droplets and peroxisomes: key players in cellular lipid homeostasis or a matter of fat--store 'em up or burn 'em down.Genetics · 2013Review
- Identification of ubiquitin-specific protease 9X (USP9X) as a deubiquitinase acting on ubiquitin-peroxin 5 (PEX5) thioester conjugate.The Journal of biological chemistry · 2012Article
- Accurate flexible fitting of high-resolution protein structures to small-angle x-ray scattering data using a coarse-grained model with implicit hydration shell.Biophysical journal · 2011Article
- PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14.The Journal of biological chemistry · 2011Article
- Versatile TPR domains accommodate different modes of target protein recognition and function.Cell stress & chaperones · 2011Review
- Normal Mode Flexible Fitting of High-Resolution Structures of Biological Molecules Toward SAXS Data.Bioinformatics and biology insights · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Pex5p receptor recognizes newly synthesized peroxisomal matrix proteins which have a C-terminal peroxisomal targeting signal to the peroxisome. After docking to protein complexes on the membrane, these proteins are translocated across the membrane. The docking mechanism remains unclear, as no structural data on the multicomponent docking complex are available. As the interaction of the cargo-loaded Pex5p receptor and the peroxisomal membrane protein Pex14p is the essential primary docking step, we have investigated the solution structure of these complexes by small angle x-ray scattering and static light scattering. Titration studies yielded a 1:6 stoichiometry for the Pex5p.Pex14p complex, and low resolution structural models were reconstructed from the x-ray scattering data. The free full-length human Pex5p is monomeric in solution, with an elongated, partially unfolded N-terminal domain. The model of the complex reveals that the N terminus of Pex5p remains extended in the presence of cargo and Pex14p, the latter proteins being significantly intermingled with the Pex5p moiety. These results suggest that the extended structure of Pex5p may play a role in interactions with other substrates such as lipids and membrane proteins during the formation of functional multiprotein complexes.
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