cleavage body

GO:0071920 · Other · Other · Proposed

A nuclear body that contains proteins involved in pre-mRNA 3'-end cleavage and polyadenylation, such as DDX1, CSTF2 and CPSFs, as well as the transcription factors TFIIE and TFIIF. Cleavage bodies are localized adjacent to Cajal bodies and are involved in mRNA3'-end processing. [GO:0071920]

Part of: nuclear lumen (GO:0031981)

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

Component	Type	Part of / acts on	Grounding	Genes	Stoichiometry	Essential	Role
CstF-64	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	CSTF2		UNKNOWN	mRNA 3'-end cleavage/polyadenylation factor that concentrates in cleavage bodies, especially during S phase. `PMID:8654386` Schul et al. 1996 identified nuclear domains containing the RNA 3' cleavage factor CstF 64 kDa close to coiled bodies. `DOI:10.1091/mbc.e05-08-0768` Li et al. 2006 used CstF-64 as a cleavage-body marker and found that CstF-64-containing cleavage bodies were primarily observed in S-phase HeLa cells.
CPSF-100	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	CPSF2		UNKNOWN	mRNA 3'-end cleavage/polyadenylation factor that marks cleavage bodies with CstF-64 and can persist in these foci into G2 phase. `PMID:8654386` Schul et al. 1996 identified CPSF 100 kDa with CstF 64 kDa in nuclear cleavage-factor domains close to coiled bodies. `DOI:10.1091/mbc.e05-08-0768` Li et al. 2006 followed CPSF-100-positive cleavage bodies in synchronized HeLa cells and their relationship to DDX1 bodies and Cajal bodies.

Taxonomic distribution

NCBITaxon:9606 Homo sapiens — VARIABLE: Cleavage bodies were defined in human cultured cells as dynamic nuclear foci enriched in CstF-64 and CPSF-100, with abundance and protein composition varying with cell-cycle state. [DOI:10.1091/mbc.10.11.3815]

Canonical examples

NCBITaxon:9606 Homo sapiens — Human T24 and HeLa cells were used to connect cleavage bodies with CstF-64/CPSF-100 concentration, nearby Cajal bodies and cell-cycle-dependent nuclear positioning. [DOI:10.1091/mbc.10.11.3815]

Functions

mRNA 3'-end processing GO:0031124 — Cleavage bodies concentrate CstF-64 and CPSF-100, proteins involved in pre-mRNA 3'-end cleavage and polyadenylation, in dynamic nuclear foci associated with Cajal bodies and S-phase histone loci.
- GO:0071920 GO:0071920 defines cleavage bodies as nuclear bodies involved in mRNA 3'-end processing and containing proteins involved in pre-mRNA 3'-end cleavage and polyadenylation.
- DOI:10.1091/mbc.10.11.3815 Schul et al. 1999 analyzed CstF-64-positive cleavage bodies beside coiled bodies and their cell-cycle-dependent overlap with the human histone gene cluster.

Mechanism graphs

CstF/CPSF concentrate in dynamic cleavage bodies (FUNCTION)

Human cleavage bodies concentrate the mRNA 3'-end-processing factors CstF-64 and CPSF-100 in nuclear foci that associate with Cajal bodies and overlap S-phase histone gene clusters.

Subject	Predicate	Object	Evidence
CstF-64	localizes to	cleavage body	`PMID:8654386` Schul et al. 1996 identified CstF-64-positive nuclear cleavage-factor domains near coiled bodies.
CPSF-100	localizes to	cleavage body	`PMID:8654386` Schul et al. 1996 identified CPSF-100-positive nuclear cleavage-factor domains near coiled bodies.
cleavage body	associates with	Cajal body	`DOI:10.1091/mbc.10.11.3815` Schul et al. 1999 followed CstF-64-positive cleavage bodies and p80-coilin-positive coiled bodies through the human T24 cell cycle.
cleavage body	overlaps	histone gene cluster	`DOI:10.1091/mbc.10.11.3815` Schul et al. 1999 detected frequent overlap between cleavage bodies and the chromosome 6p21 histone gene cluster in S-phase T24 cells.
cleavage body	concentrates factors for	mRNA 3'-end processing	`GO:0071920` GO:0071920 defines cleavage bodies as containing proteins involved in pre-mRNA 3'-end cleavage and polyadenylation.

Discussions

CURATION_TODO (OPEN): Resolve exact source-neutral protein families and additional resident versus neighboring factors of cleavage bodies. This first GO:0071920 record captures the repeatedly imaged CstF-64 and CPSF-100 cleavage-factor markers while leaving exact family groundings and the boundary around DDX1 bodies, TFIIE, TFIIF, RNA polymerase II, hnRNP K and latrunculin-induced nuclear spicules to a separate curation pass.

Evidence

GO:0071920 Gene Ontology cellular-component term for cleavage body, with definition provenance from PMID:8654386, PMID:11598190 and PMID:10564273.
GO:0016604 Gene Ontology cellular-component parent term for nuclear body.
GO:0031981 Gene Ontology cellular-component term for nuclear lumen; cleavage bodies are nuclear foci.
GO:0031124 Gene Ontology biological-process term for mRNA 3'-end processing.
PMID:8654386 Schul, Groenhout, Koberna and colleagues 1996, The RNA 3' cleavage factors CstF 64 kDa and CPSF 100 kDa are concentrated in nuclear domains closely associated with coiled bodies and newly synthesized RNA, EMBO Journal.
DOI:10.1091/mbc.10.11.3815 Schul, van der Kraan, Matera and colleagues 1999, Nuclear Domains Enriched in RNA 3'-processing Factors Associate with Coiled Bodies and Histone Genes in a Cell Cycle-dependent Manner, Molecular Biology of the Cell.
DOI:10.1091/mbc.e05-08-0768 Li, Roy, Katyal and colleagues 2006, Dynamic Nature of Cleavage Bodies and Their Spatial Relationship to DDX1 Bodies, Cajal Bodies, and Gems, Molecular Biology of the Cell.
DOI:10.1091/mbc.12.10.3046 Bleoo et al. 2001 connected human DDX1 with CstF in pre-mRNA 3'-end processing, informing the open DDX1 boundary question for cleavage-body curation.

Curation history

2026-09-28T03:51:53Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-09-28T03:53:39Z codex · EXPANDED_RECORD — Added nuclear-body parentage, nuclear-lumen parthood, CstF-64/CPSF-100 components, human cleavage-body scope, mRNA 3'-end-processing context, a nonmechanistic cleavage-body positioning graph and a component-boundary TODO.
2026-09-28T04:11:04Z codex · RESOLVED_REVIEW — Resolved #1701 by moving cleavage body from RIBONUCLEOPROTEIN to OTHER because this first record models a protein-rich nuclear body rather than a resident-RNA ribonucleoprotein granule.

Source: data/structures/other/cleavage_body.yaml