Ask about this productRelated genes to: PEX5 antibody
- Gene:
- PEX5 NIH gene
- Name:
- peroxisomal biogenesis factor 5
- Previous symbol:
- PXR1
- Synonyms:
- PTS1R
- Chromosome:
- 12p13.31
- Locus Type:
- gene with protein product
- Date approved:
- 1994-12-13
- Date modifiied:
- 2017-07-07
- Gene:
- PEX5L NIH gene
- Name:
- peroxisomal biogenesis factor 5 like
- Previous symbol:
- -
- Synonyms:
- PEX5R, PXR2, TRIP8b
- Chromosome:
- 3q26.33
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-26
- Date modifiied:
- 2016-10-05
Related products to: PEX5 antibody
Related articles to: PEX5 antibody
- For a long time, the isolation of native protein complexes from human cells was accomplished by immunoprecipitation experiments. However, success depends on the quality of the antibodies and the method consumes valuable antibodies, which can hinder subsequent analysis of the isolated complexes. Here, we demonstrate an alternative approach based on affinity purification. It utilizes human Flp-In cells, which genomically express a Protein A-tagged version of the human peroxisomal import receptor PEX5L. Native soluble and membrane-bound complexes containing PEX5L can thereby be isolated via a well-known affinity-based strategy. - Source: PubMed
Peschel RebeccaSchmidt NadineSchliebs WolfgangErdmann Ralf - The assembly of the peroxisomal translocon involves the transition of a soluble form of the peroxisomal targeting receptor PEX5 into a membrane-bound form, which becomes an integral membrane component of the import pore for peroxisomal matrix proteins. How this transition occurs is still a mystery. We addressed this question using a artificial horizontal bilayer in combination with fluorescence time-correlated single photon counting (TCSPC) and electrophysiological channel recording. Purified human isoform PEX5L and truncated PEX5L(1-335) lacking the cargo binding domain were selectively labeled with thiol-reactive Atto-dyes. Diffusion coefficients of labeled protein in solution show that PEX5L is monomeric with a rather compact spherical conformation, while the truncated protein appeared in a more extended conformation. Labeled PEX5L and the truncated PEX5L(1-335) bind stably to horizontal bilayer thereby accumulating around 100-fold. The diffusion coefficients of the membrane-bound PEX5L forms are 3-4 times lower than in solution, indicating the formation of larger complexes. Electrophysiological single channel recording shows that membrane-bound labeled and non-labeled PEX5L, but not the truncated PEX5L(1-335), can form ion conducting membrane channels. The data suggest that PEX5L is the pore-forming component of the oligomeric peroxisomal translocon and that spontaneous PEX5L membrane surface binding might be an important step in its assembly. - Source: PubMed
Publication date: 2022/10/20
Blum DanielReuter MarenSchliebs WolfgangTomaschewski JanaErdmann RalfWagner Richard - Tetratricopeptide repeat (TPR) domains are ubiquitous structural motifs that mediate protein-protein interactions. For example, the TPR domains in the peroxisomal import receptor PEX5 enable binding to a range of type 1 peroxisomal targeting signal motifs. A homolog of PEX5, tetratricopeptide repeat-containing Rab8b-interacting protein (TRIP8b), binds to and functions as an auxiliary subunit of hyperpolarization-activated cyclic nucleotide (HCN)-gated channels. Given the similarity between TRIP8b and PEX5, this difference in function raises the question of what mechanism accounts for their binding specificity. In this report, we found that the cyclic nucleotide-binding domain and the C terminus of the HCN channel are critical for conferring specificity to TRIP8b binding. We show that TRIP8b binds the HCN cyclic nucleotide-binding domain through a 37-residue domain and the HCN C terminus through the TPR domains. Using a combination of fluorescence polarization- and co-immunoprecipitation-based assays, we establish that binding at either site increases affinity at the other. Thus, allosteric coupling of the TRIP8b TPR domains both promotes binding to HCN channels and limits binding to type 1 peroxisomal targeting signal substrates. These results raise the possibility that other TPR domains may be similarly influenced by allosteric mechanisms as a general feature of protein-protein interactions. - Source: PubMed
Publication date: 2017/09/08
Lyman Kyle AHan YeHeuermann Robert JCheng XiangyingKurz Jonathan ELyman Reagan EVan Veldhoven Paul PChetkovich Dane M - - Source: PubMed
Lyman Kyle AHan YeChetkovich Dane M - The import of proteins into peroxisomes possesses many unusual features such as the ability to import folded proteins, and a surprising diversity of targeting signals with differing affinities that can be recognized by the same receptor. As understanding of the structure and function of many components of the protein import machinery has grown, an increasingly complex network of factors affecting each step of the import pathway has emerged. Structural studies have revealed the presence of additional interactions between cargo proteins and the PEX5 receptor that affect import potential, with a subtle network of cargo-induced conformational changes in PEX5 being involved in the import process. Biochemical studies have also indicated an interdependence of receptor-cargo import with release of unloaded receptor from the peroxisome. Here, we provide an update on recent literature concerning mechanisms of protein import into peroxisomes. - Source: PubMed
Baker AlisonLanyon-Hogg ThomasWarriner Stuart L