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Publication Abstract from PubMed

In the nematode Caenorhabditis elegans, sperm-derived mitochondria and membranous organelles (MOs) are selectively degraded by autophagy in embryos in a process termed allophagy. For this process, ALLO-1 functions as an autophagy adaptor. The allo-1 gene encodes two splice isoforms, ALLO-1a and b, which have different C-terminal sequences and are predominantly targeted to MOs and paternal mitochondria, respectively. However, the mechanism by which ALLO-1 targets the paternal organelles remains unknown. In this study, X-ray crystallography analysis reveals that the C-terminal region of ALLO-1a forms a parallel coiled-coil structure. In addition, Alphafold-Multimer predicts that this region directly interacts with ubiquitin. We showed that ALLO-1a interacts with K48- and K63-linked polyubiquitin in vitro and found that the 355th Asp residue of ALLO-1a at the predicted interface with ubiquitin is important for its ubiquitin binding in vitro and also for its MO-targeting and MO degradation in embryos. These results suggest that ubiquitin is a marker for the recognition of MOs by the autophagy machinery in C. elegans embryos.

ALLO-1a is a ubiquitin-binding adaptor for allophagy in Caenorhabditis elegans.,Norizuki T, Kushida Y, Sekimoto T, Sasaki T, Yamano K, Matsuda N, Sasaki R, Noda NN, Sato K, Sato M J Cell Sci. 2025 Nov 14:jcs.264252. doi: 10.1242/jcs.264252. PMID:41234204^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.