Finding the midzone: the role of ubiquitination for CPC localization during anaphase

Maerki, Sarah; Beck, Jochen; Sumara, Izabela; Peter, Matthias

doi:10.4161/cc.9.15.12740

Cited by 9 publications

(9 citation statements)

References 9 publications

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“…The top hit containing a Ser residue at the S3 position is a regulator of sister chromatid cohesion (Pds5B) (Losada et al, 2005;Panizza et al, 2000;Shintomi and Hirano, 2009). The ubiquitin-conjugating enzyme E2 L3 (UbcH7) is another interesting hit, given the finding that ubiquitination promotes the association of Survivin with centromeres during early mitosis and the dissociation at later mitotic stages (Maerki et al, 2010;Vong et al, 2005). The top hit containing a phosphomimic residue at the S3 position is hSgo1, a critical player in sister chromatid cohesion in meiosis and an interacting partner of the CPC in mitosis (Kawashima et al, 2007;Tsukahara et al, 2010;Yamagishi et al, 2010).…”

Section: Survivin-binding Motifs Are Present In Different Proteins Inmentioning

confidence: 99%

Structural Basis for the Recognition of Phosphorylated Histone H3 by the Survivin Subunit of the Chromosomal Passenger Complex

et al. 2011

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Localization of the chromosomal passenger complex (CPC) at centromeres during early mitosis is essential for accurate chromosome segregation and is dependent on the phosphorylation of histone H3. We report the 2.7 Å resolution structure of the CPC subunit Survivin bound to the N-terminal tail of histone H3 carrying the Thr3 phosphorylation mark (Thr3ph). The BIR domain of Survivin recognizes the Ala1-Arg2-Thr3ph-Lys4 sequence, decoding the modification state and the free N terminus of histone H3 by a strategy similar to that used by PHD fingers. The structural analysis permitted the identification of putative Survivin-binding epitopes in other mitotic proteins, including human Shugoshin 1. Using biophysical and structural data, we show that a phospho-mimic N-terminal sequence such as that of hSgo1 (Ala1-Lys2-Glu3-Arg4) contains the specificity determinants to bind Survivin. Our findings suggest that the CPC engages in mutually exclusive interactions with other constituents of the mitotic machinery and a histone mark in chromatin.

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Section: Survivin-binding Motifs Are Present In Different Proteins Inmentioning

confidence: 99%

Structural Basis for the Recognition of Phosphorylated Histone H3 by the Survivin Subunit of the Chromosomal Passenger Complex

et al. 2011

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“…7,[15][16][17][18][19] There are many studies on SCF E3 ligase (Skp-Cullin1-F-box protein) complex functions during mitosis, especially with regard to centrosome expression, raising the possibility that this E3 ligase family targets Aurora A. For example, the SCF β-trcp complex has roles in centrosome stability and mitotic progression; 20,21 SCF FBXL17 complex is involved in cell cycle regulation during male gametogenesis in Arabidopsis thaliana; 22 SCF cyclinF complex controls centrosome homeostasis and mitotic fidelity through CP110 degradation, 23 and SCF FBXW5 E3-ubiquitin ligase targets HsSAS-6 to control centrosome duplication.…”

Section: Introductionmentioning

confidence: 99%

Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A, causing mitotic arrest

et al. 2012

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“…While KEAP1 is oxidized on the specific cysteine residues, 13 , 23 KLHL20 is sequestered away from the substrate into PML nuclear bodies under IFN-stress conditions 21 . Interestingly, subcellular localization of other mitotic BTB-Kelch proteins involved in CUL3 complexes appears to be regulated in a timely manner during cell cycle progression 1 , 22 , 24 , 25 …”

Section: Resultsmentioning

confidence: 99%

CUL3 and protein kinases: Insights from PLK1/KLHL22 interaction

Metzger¹,

Kleiss²,

Sumara³

2013

Cell Cycle

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Posttranslational mechanisms drive fidelity of cellular processes. Phosphorylation and ubiquitination of substrates represent very common, covalent, posttranslational modifications and are often co-regulated. Phosphorylation may play a critical role both by directly regulating E3-ubiquitin ligases and/or by ensuring specificity of the ubiquitination substrate. Importantly, many kinases are not only critical regulatory components of these pathways but also represent themselves the direct ubiquitination substrates. Recent data suggest the role of CUL3-based ligases in both proteolytic and non-proteolytic regulation of protein kinases. Our own recent study identified the mitotic kinase PLK1 as a direct target of the CUL3 E3-ligase complex containing BTB-KELCH adaptor protein KLHL22.1 In this study, we aim at gaining mechanistic insights into CUL3-mediated regulation of the substrates, in particular protein kinases, by analyzing mechanisms of interaction between KLHL22 and PLK1. We find that kinase activity of PLK1 is redundant for its targeting for CUL3-ubiquitination. Moreover, CUL3/KLHL22 may contact 2 distinct motifs within PLK1 protein, consistent with the bivalent mode of substrate targeting found in other CUL3-based complexes. We discuss these findings in the context of the existing knowledge on other protein kinases and substrates targeted by CUL3-based E3-ligases.

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Finding the midzone: the role of ubiquitination for CPC localization during anaphase

Cited by 9 publications

References 9 publications

Structural Basis for the Recognition of Phosphorylated Histone H3 by the Survivin Subunit of the Chromosomal Passenger Complex

Structural Basis for the Recognition of Phosphorylated Histone H3 by the Survivin Subunit of the Chromosomal Passenger Complex

Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A, causing mitotic arrest

CUL3 and protein kinases: Insights from PLK1/KLHL22 interaction

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