Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1931725 | Biochemical and Biophysical Research Communications | 2010 | 5 Pages |
Abstract
We previously reported the identification of DP-1 isoforms (α and β), which are structurally C-terminus-deleted ones, and revealed the low-level expression of these isoforms. It is known that wild-type DP-1 is degraded by the ubiquitin–proteasome system, but few details are known about the domains concerned with the protein stability/instability for the proteolysis of these DP-1 isoforms. Here we identified the domains responsible for the stability/instability of DP-1. Especially, the DP-1 “Stabilon” domain was a C-terminal acidic motif and was quite important for DP-1 stability. Moreover, we propose that this DP-1 Stabilon may be useful for the stability of other nuclear proteins when fused to them.
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Authors
Takashi Arakawa, Yoshikazu Masuhiro, Yoshiaki Kamiya, Hirohisa Kojima, Shigemasa Hanazawa,