Matthias Wilmanns
LightNews LightNews
matthiaswilmanns.bsky.social
Matthias Wilmanns
@matthiaswilmanns.bsky.social
110 followers 48 following 2 posts
EMBL Senior Scientist, Group Leader
Posts Replies Media Videos
matthiaswilmanns.bsky.social
We are excited to share our latest work, where we unravel the structural and functional secrets of the once-mysterious protein Pex8 revealing how it controls the peroxisomal cargo import receptor Pex5.

Read more here: www.biorxiv.org/content/10.1101/2025.08.30.673231v1
Ensemble model of the full length Pex5 receptor (different blue color) in complex with Pex8 (green colors). Key Findings: Pex8 binds to a novel site on the mostly unfolded N-terminal region of the Pex5 receptor. This interaction is essential for peroxisomal protein import. Computational modelling reveals the formation of an assembly with the trimeric peroxisomal E3-ubiquitin ligase. We propose that this action positions the Pex5 receptor for its recycling, a step essential for the entire protein import process. Why this matters: Peroxisomes rely entirely on the import of folded proteins to function. Impaired peroxisome function is linked to severe disorders, and recent data show their crucial roles in carcinogenesis and the immune response. Our work elevates Pex8 from an enigma to a central player in this critical biological process. Read the full story and see the structures here: https://www.biorxiv.org/content/10.1101/2025.08.30.673231v1 #CellBiology #StructuralBiology #Peroxisome #ProteinImport #bioRxiv #Biochemistry
September 3, 2025 at 10:28 AM