The eukaryotic defective in cullin neddylation (DCN) protein family, contributes to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. These multi-protein complexes are required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome[, , ]. Proteins in the DCN family include:Yeast DCN1.Vertebrate DCN1-like protein 1-5.Plant Defective in cullin neddylation protein AAR3 [].DCN family proteins all contain a Potentiating neddylation (PONY) domain (), contains a cullin-binding surface within its C-terminal region and is sufficient to promote neddylation [, ]. The N-terminal region of the protein often contains a UBA-like domain.
This domain is found in the eukaryotic family defective in cullin neddylation, which includes DCN1 and DCN1-like proteins. Proteins of the DCN family may contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes, which are multi-protein complexes required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome [, ].The structure of this domain is composed entirely of alpha helices [, ]. It has been referred to as potentiating neddylation domain (PONY) and can be found in association with an N-terminal UBA domain. The PONY domain contains a cullin-binding surface within its C-terminal region and is sufficient to promote neddylation [, ].
This superfamily represents a domain is found in DCN1-like proteins. Proteins of the DCN family may contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes, which are multi-protein complexes required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome [, ].The structure of this domain is composed entirely of alpha helices [, ]. It has been referred to as potentiating neddylation domain (PONY) and can be found in association with an N-terminal UBA domain. The PONY domain contains a cullin-binding surface within its C-terminal region and is sufficient to promote neddylation [, ].
