UFD2a is a mammalian homolog of Saccharomyces cerevisiae Ufd2, originally described as an E4 ubiquitination factor. UFD2a belongs to the U-box family of ubiquitin ligases (E3s) and likely functions as both an E3 and E4. We have isolated and characterized the mouse gene (Ube4b) for UFD2a. A full-length (∼5700bp) Ube4b cDNA was isolated and the corresponding gene spans 100kb, comprising 27 exons. Luciferase reporter gene analysis of the 5 ′ flanking region of Ube4b revealed that nucleotides -1018 to -943 (relative to the translation initiation site) possess promoter activity. This functional sequence contains two putative Sp1 binding sites but not a TATA box. Immunoblot and immunohistochemical analyses revealed that UFD2a is expressed predominantly in the neuronal tissues. We also show that UFD2a interacts with VCP (a AAA-family ATPase) that is thought to mediate protein folding. These data implicate UFD2a in the degradation of neuronal proteins by the ubiquitin-proteasome pathway.
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - Jan 10 2003|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology