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The E3 ligase CUL3/RDX controls centromere maintenance by ubiquitylating and stabilizing CENP-A in a CAL1-dependent manner

Centromeres are defined by the presence of the histone H3 variant CENP-A in a subset of centromeric nucleosomes. CENP-A deposition to centromeres depends on a specialized loading factor from yeast to humans that is called CAL1 in Drosophila. Here, we show that CAL1 directly interacts with RDX, an ad...

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Main Authors: Bade, Debora (Author) , Pauleau, Anne-Laure (Author) , Wendler, Astrid (Author) , Erhardt, Sylvia (Author)
Format: Article (Journal)
Language:English
Published: March 10, 2014
In: Developmental cell
Year: 2014, Volume: 28, Issue: 5, Pages: 508-519
ISSN:1878-1551
DOI:10.1016/j.devcel.2014.01.031
Online Access:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1016/j.devcel.2014.01.031
Verlag, kostenfrei, Volltext: http://www.sciencedirect.com/science/article/pii/S1534580714000720
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Author Notes:Debora Bade, Anne-Laure Pauleau, Astrid Wendler, and Sylvia Erhardt

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520 |a Centromeres are defined by the presence of the histone H3 variant CENP-A in a subset of centromeric nucleosomes. CENP-A deposition to centromeres depends on a specialized loading factor from yeast to humans that is called CAL1 in Drosophila. Here, we show that CAL1 directly interacts with RDX, an adaptor for CUL3-mediated ubiquitylation. However, CAL1 is not a substrate of the CUL3/RDX ligase but functions as an additional substrate-specifying factor for the CUL3/RDX-mediated ubiquitylation of CENP-A. Remarkably, ubiquitylation of CENP-A by CUL3/RDX does not trigger its degradation but stabilizes CENP-A and CAL1. Loss of RDX leads to a rapid degradation of CAL1 and CENP-A and to massive chromosome segregation defects during development. Essentially, we identified a proteolysis-independent role of ubiquitin conjugation in centromere regulation that is essential for the maintenance of the centromere-defining protein CENP-A and its loading factor CAL1. 
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