| RRC ID |
86860
|
| Author |
Norizuki T, Kushida Y, Sekimoto T, Sasaki T, Yamano K, Matsuda N, Sasaki R, Noda NN, Sato K, Sato M.
|
| Title |
ALLO-1a is a ubiquitin-binding adaptor for allophagy in Caenorhabditis elegans.
|
| Journal |
J Cell Sci
|
| Abstract |
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 ALLO-1b, 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, AlphaFold2-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 D355 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.
|
| Volume |
138(24)
|
| Published |
2025-12-15
|
| DOI |
10.1242/jcs.264252
|
| PII |
369838
|
| PMID |
41234204
|
| MeSH |
Animals
Autophagy*
Caenorhabditis elegans* / embryology
Caenorhabditis elegans* / genetics
Caenorhabditis elegans* / metabolism
Caenorhabditis elegans Proteins* / chemistry
Caenorhabditis elegans Proteins* / genetics
Caenorhabditis elegans Proteins* / metabolism
Embryo, Nonmammalian / metabolism
Mitochondria / metabolism
Protein Binding
Ubiquitin* / metabolism
|
| IF |
4.573
|
| Resource |
| DNA material |
CSII-CMV-MCS-IRES2-Bsd (RDB04385)
pCAG-HIVgp (RDB04394)
pCMV-VSV-G-RSV-Rev (RDB04393) |
