The E3 Ligase CUL3/RDX Controls Centromere Maintenance by Ubiquitylating and Stabilizing CENP-A in a CAL1-Dependent Manner

Bade, Debora; Pauleau, Anne-Laure; Wendler, Astrid; Erhardt, Sylvia

doi:10.1016/j.devcel.2014.01.031

Cited by 43 publications

(54 citation statements)

References 40 publications

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“…RDX monoubiquitylates CENP-A/CID, which stabilizes CENP-A/CID and the HJURP ortholog CAL1 (Bade et al, 2014). Whether mammalian CRL3 similarly regulates the stability of CENP-A and/or HJURP remains to be determined.…”

Section: Automated Image Analysis Quantifies Levels and Dynamics Of Cmentioning

confidence: 99%

“…Clearly, it would be of prime interest to identify the crucial CRL4 RBBP7 substrates. Recent work in Drosophila has identified CENP-A as a potential candidate (Bade et al, 2014), and it is possible that ubiquitylation of newly synthesized CENP-A is required for its centromere deposition. Another line of questioning derives from the observation that centromeric regions are enriched in histone methylation and display a low degree of acetylation, which appears to influence the structural organization of chromatin (Bergmann et al, 2011;Kim et al, 2012;Ohzeki et al, 2012).…”

Section: Crl4 Is Not Required To Regulate Deposition Of Other Histonementioning

confidence: 99%

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CRL4RBBP7 is required for efficient CENP-A deposition at centromeres

Mouysset¹,

Gilberto²,

Meier³

et al. 2015

Journal of Cell Science

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The mitotic spindle drives chromosome movement during mitosis and attaches to chromosomes at dedicated genomic loci named centromeres. Centromeres are epigenetically specified by their histone composition, namely the presence of the histone H3 variant CENP-A, which is regulated during the cell cycle by its dynamic expression and localization. Here, we combined biochemical methods and quantitative imaging approaches to investigate a new function of CUL4-RING E3 ubiquitin ligases (CRL4) in regulating CENP-A dynamics. We found that the core components CUL4 and DDB1 are required for centromeric loading of CENP-A, but do not influence CENP-A maintenance or pre-nucleosomal CENP-A levels. Interestingly, we identified RBBP7 as a substrate-specific CRL4 adaptor required for this process, in addition to its role in binding and stabilizing soluble CENP-A. Our data thus suggest that the CRL4 complex containing RBBP7 (CRL4 RBBP7 ) might regulate mitosis by promoting ubiquitin-dependent loading of newly synthesized CENP-A during the G1 phase of the cell cycle.

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Section: Automated Image Analysis Quantifies Levels and Dynamics Of Cmentioning

confidence: 99%

Section: Crl4 Is Not Required To Regulate Deposition Of Other Histonementioning

confidence: 99%

CRL4RBBP7 is required for efficient CENP-A deposition at centromeres

Mouysset¹,

Gilberto²,

Meier³

et al. 2015

Journal of Cell Science

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“…Ubiquitylation of dCENP-A CID is distinguished by the fact that the E3 ligase CUL3/RDX1 complex directly interacts with the functional homolog of HJURP in flies, called CAL1, which serves as an adaptor for the enzymatic reaction (Bade et al 2014; Chen et al 2014; Erhardt et al 2008). CAL1 itself does not undergo ubiquitylation; nonetheless, both CAL1 and dCENP-A CID are stabilized by the CUL3/RDX complex, and loss of RDX leads to fragmented chromosomes and perturbs centromere maintenance.…”

Section: Diversity Of Cenp-a Modifications Across Speciesmentioning

confidence: 99%

Posttranslational modifications of CENP-A: marks of distinction

Srivastava

Foltz

2018

Chromosoma

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Centromeres are specialized chromosome domain that serve as the site for kinetochore assembly and microtubule attachment during cell division, to ensure proper segregation of chromosomes. In higher eukaryotes, the identity of active centromeres is marked by the presence of CENP-A (centromeric protein-A), a histone H3 variant. CENP-A forms a centromere-specific nucleosome that acts as a foundation for centromere assembly and function. The posttranslational modification (PTM) of histone proteins is a major mechanism regulating the function of chromatin. While a few CENP-A site-specific modifications are shared with histone H3, the majority are specific to CENP-A-containing nucleosomes, indicating that modification of these residues contribute to centromere-specific function. CENP-A undergoes posttranslational modifications including phosphorylation, acetylation, methylation, and ubiquitylation. Work from many laboratories have uncovered the importance of these CENP-A modifications in its deposition at centromeres, protein stability, and recruitment of the CCAN (constitutive centromere-associated network). Here, we discuss the PTMs of CENP-A and their biological relevance.

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“…These data suggest that mechanisms exist to detect and degrade Scm3-free CENP-A Cse4 to prevent incorrect assembly. The role of CENP-A ubiquitination in regulating CENP-A assembly may be conserved, as ubiquitination of Drosophila CENP-A CID by the E3 ubiquitin ligases Ppa and CUL3 can destabilize or stabilize CENP-A CID , respectively (Moreno-Moreno et al 2011;Bade et al 2014).…”

Section: Additional Factors Involved In Cenp-a Assemblymentioning

confidence: 99%

“…Histone modification of non-CENP-A nucleosomes is therefore likely to have a role in centromere maintenance and function. In addition, CENP-A nucleosomes themselves are likely to be subject to modification; CENP-A ubiquitination by CUL3/RDX ubiquitin ligase has been shown to stabilize soluble CENP-A in Drosophila (Bade et al 2014). …”

Section: Histone Modificationsmentioning

confidence: 99%

The Centromere: Epigenetic Control of Chromosome Segregation during Mitosis

Westhorpe

Straight

2014

Cold Spring Harb Perspect Biol

149

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A fundamental challenge for the survival of all organisms is maintaining the integrity of the genome in all cells. Cells must therefore segregate their replicated genome equally during each cell division. Eukaryotic organisms package their genome into a number of physically distinct chromosomes, which replicate during S phase and condense during prophase of mitosis to form paired sister chromatids. During mitosis, cells form a physical connection between each sister chromatid and microtubules of the mitotic spindle, which segregate one copy of each chromatid to each new daughter cell. The centromere is the DNA locus on each chromosome that creates the site of this connection. In this review, we present a brief history of centromere research and discuss our current knowledge of centromere establishment, maintenance, composition, structure, and function in mitosis.

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The E3 Ligase CUL3/RDX Controls Centromere Maintenance by Ubiquitylating and Stabilizing CENP-A in a CAL1-Dependent Manner

Cited by 43 publications

References 40 publications

CRL4RBBP7 is required for efficient CENP-A deposition at centromeres

CRL4RBBP7 is required for efficient CENP-A deposition at centromeres

Posttranslational modifications of CENP-A: marks of distinction

The Centromere: Epigenetic Control of Chromosome Segregation during Mitosis

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