ArticleThe Journal of cell biology2022
Prion-like domains drive CIZ1 assembly formation at the inactive X chromosome.
Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Modification of internal RNA domains from the long non-coding RNA XIST refines roles in silencing and heterochromatin recruitment.Human molecular genetics · 2026Article
- AURKB-driven dissolution of CIZ1-RNA assemblies from the inactive X chromosome in mitosis.Nucleic acids research · 2026Article
- Implication of the Mediator kinase module in CIZ1 recruitment and gene silencing byEpigenetics reports · 2025Article
- Impact of somatic XIST deletions on ongoing XIST expression and inactive X silencing and heterochromatin.Human molecular genetics · 2025Article
- Phase separation paints Xi with Xist.Cell research · 2025Article
- Role of the SAF-A/HNRNPU SAP domain in X chromosome inactivation, nuclear dynamics, transcription, splicing, and cell proliferation.PLoS genetics · 2025Article
- Epigenetic deprogramming by disruption of CIZ1-RNA nuclear assemblies in early-stage breast cancers.The Journal of cell biology · 2025Article
- RNA: The Unsuspected Conductor in the Orchestra of Macromolecular Crowding.Chemical reviews · 2024Review
- IndiSPENsable for X Chromosome Inactivation and Gene Silencing.Epigenomes · 2023Review
- Epigenetic instability caused by absence of CIZ1 drives transformation during quiescence cycles.BMC biology · 2023Article
- Derivation of a minimal functional XIST by combining human and mouse interaction domains.Human molecular genetics · 2023Article
- CIZ1 in Xist seeded assemblies at the inactive X chromosome.Frontiers in cell and developmental biology · 2023Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
CIZ1 forms large assemblies at the inactive X chromosome (Xi) in female fibroblasts in an Xist lncRNA-dependent manner and is required for accurate maintenance of polycomb targets genome-wide. Here we address requirements for assembly formation and show that CIZ1 undergoes two direct interactions with Xist, via independent N- and C-terminal domains. Interaction with Xist, assembly at Xi, and complexity of self-assemblies formed in vitro are modulated by two alternatively spliced glutamine-rich prion-like domains (PLD1 and 2). PLD2 is dispensable for accumulation at existing CIZ1-Xi assemblies in wild-type cells but is required in CIZ1-null cells where targeting, assembly, and enrichment for H3K27me3 and H2AK119ub occur de novo. In contrast, PLD1 is required for both de novo assembly and accumulation at preexisting assemblies and, in vitro, drives formation of a stable fibrillar network. Together they impart affinity for RNA and a complex relationship with repeat E of Xist. These data show that alternative splicing of two PLDs modulates CIZ1's ability to build large RNA-protein assemblies.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.