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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
RBBP6 Interacts with Multifunctional Protein YB-1 through Its RING Finger Domain, Leading to Ubiquitination and Proteosomal Degradation of YB-1
Journal of Molecular Biology, Volume 384, No. 4, Year 2008
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Description
RBBP6 (retinoblastoma binding protein 6) is a 250-kDa multifunctional protein that interacts with both p53 and pRb and has been implicated in mRNA processing. It has also been identified as a putative E3 ubiquitin ligase due to the presence of a RING finger domain, although no substrate has been identified up to now. Using the RING finger domain as bait in a yeast two-hybrid screen, we identified YB-1 (Y-box binding protein 1) as a binding partner of RBBP6, localising the interaction to the last 62 residues of YB-1. We showed, furthermore, that both full-length RBBP6 and the isolated RING finger domain were able to ubiquitinate YB-1, resulting in its degradation in the proteosome. As a result, RBBP6 was able to suppress the levels of YB-1 in vivo and to reduce its transactivational ability. In the light of the important role that YB-1 appears to play in tumourigenesis, our results suggest that RBBP6 may be a relevant target for therapeutic drugs aimed at modifying the activity of YB-1. © 2008 Elsevier Ltd. All rights reserved.
Authors & Co-Authors
Chibi, Moredreck
South Africa, Bellville
University of the Western Cape
Meyer, Mervin E.
South Africa, Bellville
University of the Western Cape
Skepu, Amanda
South Africa, Tygerberg
South African Medical Research Council
Rees, David Jasper Gilbert
South Africa, Bellville
University of the Western Cape
Moolman-Smook, Johanna Catharina
South Africa, Stellenbosch
Stellenbosch University
Pugh, David J.R.
South Africa, Bellville
University of the Western Cape
Statistics
Citations: 90
Authors: 6
Affiliations: 3
Identifiers
Doi:
10.1016/j.jmb.2008.09.060
ISSN:
00222836