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Itch/AIP4 mediates Deltex degradation through the formation of K29‐linked polyubiquitin chains
Author(s) -
Chastagner Patricia,
Israël Alain,
Brou Christel
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400822
Subject(s) - ubiquitin , ubiquitin ligase , microbiology and biotechnology , endocytic cycle , biology , notch signaling pathway , drosophila melanogaster , gene , biochemistry , signal transduction , receptor , endocytosis
Deltex (DTX) and AIP4 are the human orthologues of the Drosophila deltex and Suppressor of deltex, which have been genetically described as being antagonistically involved in the Notch signalling pathway. Both genes encode E3 ubiquitin ligases of the RING (Really interesting new gene)‐H2 and HECT (Homologous to E6AP carboxyl terminus) families, respectively. In an attempt to understand the molecular basis of their genetic interactions, we studied the relationship between DTX and AIP4 in the absence of activation of the Notch pathway. We show here that both molecules interact and partially colocalize to endocytic vesicles, and that AIP4 targets DTX for lysosomal degradation. Furthermore, AIP4‐generated polyubiquitin chains are mainly conjugated through lysine 29 of ubiquitin in vivo , indicating a link between this type of chain and lysosomal degradation.