CED-6 is a phosphotyrosine-binding (PTB) domain-containing protein conserved in humans (Homo sapiens), mice (Mus musculus), and rats (Rattus norvegicus). It acts as an adaptor molecule in signaling pathways for engulfing apoptotic cells and participates in clathrin-associated endocytic processes . Key features include:
CED-6 facilitates phagocytosis by acting as a downstream effector of CED-1, a transmembrane receptor. In C. elegans, ced-6 mutants exhibit defective apoptotic cell clearance . The protein’s PTB domain binds to CED-1’s cytoplasmic tail, triggering Rac1 activation and cytoskeletal reorganization .
CED-6 interacts with clathrin and AP-2 adaptors to regulate endocytosis:
Co-localization: CED-6 localizes with clathrin-coated structures in Drosophila oocytes .
Functional Redundancy: In C. elegans, ced-6 works redundantly with AP-2 and clathrin to maintain CED-1 membrane localization .
Lipid Binding: The PTB domain binds PtdIns(4,5)P₂, enhancing membrane association .
CED-6 dysfunction is linked to:
Neurodegeneration: Altered phagocytosis in macrophages and neurons .
Reproductive Defects: Drosophila ced-6 mutants show semifertility due to defective yolk uptake .
CED-6 antibodies are used in diverse assays: