trim-21 promotes proteasomal degradation of CED-1 for apoptotic cell clearance in C. elegans

trim-21 promotes proteasomal degradation of CED-1 for apoptotic cell clearance in C. elegans

Blog Article

The phagocytic receptor CED-1 mediates apoptotic cell recognition Electrical Parts by phagocytic cells, enabling cell corpse clearance in Caenorhabditis elegans.Whether appropriate levels of CED-1 are maintained for executing the engulfment function remains unknown.Here, we identified the C.

elegans E3 ubiquitin ligase tripartite motif containing-21 (TRIM-21) as a component of the CED-1 pathway for apoptotic cell clearance.When the NPXY motif of CED-1 was bound to the adaptor protein CED-6 or the YXXL motif of CED-1 was phosphorylated by tyrosine kinase SRC-1 and subsequently bound to the adaptor protein NCK-1 containing the SH2 domain, TRIM-21 functioned in conjunction with UBC-21 to catalyze K48-linked poly-ubiquitination on CED-1, targeting it for proteasomal degradation.In the absence of TRIM-21, CED-1 accumulated post-translationally and drove cell corpse degradation defects, as evidenced by direct binding to VHA-10.

These findings HIBISCUS reveal a unique mechanism for the maintenance of appropriate levels of CED-1 to regulate apoptotic cell clearance.