ArticleEMBO reports2016
Centromere localization and function of Mis18 requires Yippee-like domain-mediated oligomerization.
Article in EMBO reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Structural basis of βKNL2 centromeric targeting mechanism and its role in plant-specific kinetochore assembly.Nucleic acids research · 2026Article
- M18BP1 valency and a distributed interaction footprint determine epigenetic centromere specification in humans.The EMBO journal · 2026Article
- Dual pathways via CENP-C and Mis18C recruit HJURP for CENP-A deposition into vertebrate centromeres.The EMBO journal · 2026Article
- Yippee-like protein Moh1 links gene expression to metabolism and selective stress resistance inMicrobial cell (Graz, Austria) · 2026Article
- Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025Review
- Exploring the structural landscape of DNA maintenance proteins.Nature communications · 2024Article
- Structural basis for Mis18 complex assembly and its implications for centromere maintenance.EMBO reports · 2024Article
- The cysteine-rich domain in CENP-A chaperone Scm3HJURP ensures centromere targeting and kinetochore integrity.Nucleic acids research · 2024Article
- Dynamic proximity interaction profiling suggests that YPEL2 is involved in cellular stress surveillance.Protein science : a publication of the Protein Society · 2024Article
- β-TrCP-Mediated Proteolysis of Mis18β Prevents Mislocalization of CENP-A and Chromosomal Instability.Molecular and cellular biology · 2024Article
- Direct recruitment of Mis18 to interphase spindle pole bodies promotes CENP-A chromatin assembly.Current biology : CB · 2023Article
- FREEDA: An automated computational pipeline guides experimental testing of protein innovation.The Journal of cell biology · 2023Article
- The cryo-EM structure of the CENP-A nucleosome in complex with ggKNL2.The EMBO journal · 2023Article
- FREEDA: an automated computational pipeline guides experimental testing of protein innovation by detecting positive selection.bioRxiv : the preprint server for biology · 2023Article
- Centromere targeting of Mis18 requires the interaction with DNA and H2A-H2B in fission yeast.Cellular and molecular life sciences : CMLS · 2021Article
- Frameshift mutations ofDisease models & mechanisms · 2020Article
- The centromere comes into focus: from CENP-A nucleosomes to kinetochore connections with the spindle.Open biology · 2020Review
- Mechanism of centromere recruitment of the CENP-A chaperone HJURP and its implications for centromere licensing.Nature communications · 2019Article
- Subunit interactions and arrangements in the fission yeast Mis16-Mis18-Mis19 complex.Life science alliance · 2019Article
- De novo formation and epigenetic maintenance of centromere chromatin.Current opinion in cell biology · 2019Review
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Authors and funding
8 authors.
Funding
Abstract
Mis18 is a key regulator responsible for the centromere localization of the CENP-A chaperone Scm3 in Schizosaccharomyces pombe and HJURP in humans, which establishes CENP-A chromatin that defines centromeres. The molecular and structural determinants of Mis18 centromere targeting remain elusive. Here, by combining structural, biochemical, and yeast genetic studies, we show that the oligomerization of S. pombe Mis18, mediated via its conserved N-terminal Yippee-like domain, is crucial for its centromere localization and function. The crystal structure of the N-terminal Yippee-like domain reveals a fold containing a cradle-shaped pocket that is implicated in protein/nucleic acid binding, which we show is required for Mis18 function. While the N-terminal Yippee-like domain forms a homodimer in vitro and in vivo, full-length Mis18, including the C-terminal α-helical domain, forms a homotetramer in vitro We also show that the Yippee-like domains of human Mis18α/Mis18β interact to form a heterodimer, implying a conserved structural theme for Mis18 regulation.
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