Abstract:
:SIAH-1, an E3 ubiquitin ligase, plays an important role in regulating cell cycle, tumorigenesis and several neurodegenerative diseases. In this study, we found a novel SIAH-1-interacting protein, EEF1D (Eukaryotic translation elongation factor 1 delta). The interaction was confirmed in vitro and in vivo, and both proteins were co-localized in the cytoplasm. The Cys-rich domain of SIAH-1 was essential for its interaction with EEF1D. Overexpressing SIAH-1 had no effect on the protein level of EEF1D, implying that EFF1D is not the substrate of SIAH-1. In contrast, the protein level of SIAH-1 increased significantly in the cells overexpressing EEF1D. Increased amount of SIAH-1 was caused by the EEF1D-mediated inhibition of auto-ubiquitination and degradation of SIAH-1. Furthermore, EEF1D was able to inhibit the degradation of HPH2, a known substrate of SIAH-1. Taken together, our data suggest EFF1D functions as a novel negative regulator of SIAH-1.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Wu H,Shi Y,Lin Y,Qian W,Yu Y,Huo Kdoi
10.1007/s11010-011-0891-5subject
Has Abstractpub_date
2011-11-01 00:00:00pages
209-15issue
1-2eissn
0300-8177issn
1573-4919journal_volume
357pub_type
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