ufd-2 Antibody

UFD-2 acts as an E4 ubiquitin ligase, mediating the assembly of polyubiquitin chains on substrates that have been ubiquitinated by another E3 ubiquitin ligase. The elongation of preexisting ubiquitin chains preferentially targets ubiquitin 'Lys-29' and 'Lys-48' residues. UFD-2 also functions as an E3 ligase in conjunction with specific E1 and E2 ligases. It is likely that UFD-2 coordinates DNA double-strand-break repair and apoptosis in the germline by regulating protein ubiquitination at DNA damage repair sites. UFD-2 is required for germline apoptosis in response to DNA damage downstream of CEP-1. It is involved in the resolution of DNA-repair sites by promoting the release of RAD-51 from DNA damage foci. In association with the protein ligase CHN-1, UFD-2 acts as an E3/E4 ligase to poly-ubiquitinate lysine residues in the UCS domain of the myosin chaperone UNC-45. By targeting the myosin chaperone UNC-45 for proteasomal degradation, UFD-2 regulates myosin assembly in body wall muscles in association with CDC-48.1 and CHN-1. However, in a contrasting study, UFD-2 acts as an E3 ligase, independently of CHN-1, to poly-ubiquitinate UNC-45 without promoting UNC-45 proteasomal degradation. Instead, it uses UNC-45 as an adapter protein to recruit and poly-ubiquitinate unfolded myosin heavy chain B UNC-54.