Synergistic effect of two E2 ubiquitin conjugating enzymes in SCF(hFBH1) catalyzed polyubiquitination

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Title
Synergistic effect of two E2 ubiquitin conjugating enzymes in SCF(hFBH1) catalyzed polyubiquitination
Author(s)
Jeong Hoon Kim; Jin Sun Choi; Sunhong Kim; Kidae Kim; P K Myung; Sung Goo Park; Y S Seo; Byoung Chul Park
Bibliographic Citation
BMB Reports, vol. 48, no. 1, pp. 25-29
Publication Year
2015
Abstract
Ubiquitination is a post translational modification which mostly links with proteasome dependent protein degradation. This process has been known to play pivotal roles in the number of biological events including apoptosis, cell signaling, transcription and translation. Although the process of ubiquitination has been studied extensively, the mechanism of polyubiquitination by multi protein E3 ubiquitin ligase, SCF complex remains elusive. In the present study, we identified UbcH5a as a novel stimulating factor for poly-ubiquitination catalyzed by SCFhFBH1 using biochemical fractionations and MALDI-TOF. Moreover, we showed that recombinant UbcH5a and Cdc34 synergistically stimulate SCFhFBH1 catalyzed polyubiquitination in vitro. These data may provide an important cue to understand the mechanism how the SCF complex efficiently polyubiquitinates target substrates.
Keyword
E2 ubiquitin conjugating enzymehFBH1PolyubiquitinationSCFUbiquitin
ISSN
1225-8687
Publisher
South Korea
DOI
http://dx.doi.org/10.5483/BMBRep.2015.48.1.057
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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