GO:0110070 cellularization cleavage furrow: Components, Assembly and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0110070 cellularization cleavage furrow is a cellular component defined as a plasma membrane invagination at the site of separation of a multi-nucleate cell or syncytium into individual cells.
• The term captures the specialized furrow apparatus that partitions a syncytial cytoplasm into individual cells, best studied in Drosophila early embryos and chytrid fungi [1,3,4,6].
• Key molecular players include actin, Myosin II, anillin, Slam, amphiphysin, GRAF, and Dunk, which together build and regulate the furrow [1,3,5,6].
• Unlike conventional cytokinesis, cellularization cleavage furrows form around multiple nuclei simultaneously and use distinct membrane-trafficking and actomyosin-remodeling strategies [2,4,8].
• Defects in furrow components are linked to failed cell partitioning, developmental lethality, and abnormal actomyosin contractility, with broader implications for tissue morphogenesis and disease modeling [3,5,6].
• CRISPR knockout, point-mutation, knock-in, and overexpression models enable causal dissection of furrow gene function in Drosophila and fungal systems [1,3,5].
Description
GO:0110070 cellularization cleavage furrow is a Gene Ontology cellular component term that describes a plasma membrane invagination at the site of separation of a multi-nucleate cell or syncytium into individual cells. This structure is central to cellularization, the process by which a single large cell containing many nuclei is subdivided into discrete cells. In Drosophila melanogaster embryos, cellularization cleavage furrows form synchronously around thousands of nuclei at the cortex, making the embryo a powerful system for studying furrow assembly and membrane remodeling [1,3,6]. The term is also relevant to non-animal systems, as chytrid fungi undergo cellularization using mechanisms that differ from conventional cytokinesis and from animal cellularization [4,8]. Researchers study GO:0110070 because it represents a specialized membrane domain where actomyosin contractility, vesicle trafficking, and cytoskeletal anchoring converge. The furrow is not a generic cleavage furrow; it is a developmentally programmed invagination that partitions a syncytium. Work in Drosophila has shown that the BAR domain protein amphiphysin is required for cleavage furrow tip-tubule formation during cellularization, linking membrane curvature generation to furrow progression. Similarly, the RhoGTPase regulator GRAF is spatiotemporally recruited to inhibit actomyosin ring constriction during cellularization, revealing tight spatial control of contractility. Understanding this term matters for cell and developmental biologists because failures in furrow formation or regulation can disrupt cell partitioning and downstream morphogenesis. The furrow also serves as a model for studying how membrane invaginations are built and stabilized, with implications for cytokinesis, syncytial organization, and tissue architecture [2,5,6]. Because the term is a cellular component, it is best studied with imaging, proteomics, and genetic perturbation approaches that resolve where and when furrow proteins act.
cellularization cleavage furrow At A Glance
| GO ID | GO:0110070 |
|---|---|
| GO term | cellularization cleavage furrow |
| Ontology | cellular_component |
| Synonym | None listed in QuickGO |
| Definition | A plasma membrane invagination at the site of separation of a multi-nucleate cell or syncytium into individual cells. |
| Major function | Partitioning a syncytium into individual cells by inward membrane growth and actomyosin-driven remodeling. |
| Representative organisms | Drosophila melanogaster, chytrid fungi [1,3,4,6,8] |
| Key structural features | Membrane invagination, actomyosin ring, tip tubules, and associated trafficking machinery [1,3,6] |
| Related processes | Cellularization, cytokinesis, membrane trafficking, actomyosin contractility [2,4,8] |
What Is GO:0110070?
In simple terms, the cellularization cleavage furrow is the inward fold of the plasma membrane that cuts a multi-nucleate cell into separate cells. According to the QuickGO definition, it is a plasma membrane invagination at the site of separation of a multi-nucleate cell or syncytium into individual cells. This definition places the term in the cellular_component ontology aspect, meaning it describes a subcellular structure rather than a process or a molecular activity. The furrow is therefore a membrane domain with associated cytoskeletal and trafficking machinery, not merely a transient event. It is distinct from canonical cytokinetic furrows because it operates in a syncytial context and often forms around many nuclei simultaneously [1,4,6].
Why Is cellularization cleavage furrow Important in Cell Biology?
GO:0110070 is important because it defines the structural platform that converts a syncytium into a multicellular tissue. In Drosophila, cellularization cleavage furrows must form and invaginate with precise timing to enclose each nucleus, and disruption of furrow components such as amphiphysin, Slam, anillin, or Myosin II regulators leads to failed cellularization and developmental defects [1,3,5,6]. The term also provides a comparative framework for non-animal systems: chytrid fungi cellularize using mechanisms distinct from conventional cytokinesis and from animal cellularization, which broadens the evolutionary scope of furrow biology [4,8]. For researchers, this term is a useful anchor for annotating genes, designing imaging experiments, and interpreting phenotypes in syncytial tissues.
• Defines the membrane invagination that partitions a syncytium into individual cells during development [1,4].
• Provides a cellular-component anchor for annotating genes involved in cellularization and furrow assembly [3,6].
• Links actomyosin contractility to membrane remodeling through proteins such as anillin and Myosin II.
• Highlights the role of membrane curvature machinery, including the BAR domain protein amphiphysin, in furrow tip-tubule formation.
• Reveals spatiotemporal inhibition of actomyosin ring constriction by RhoGTPase regulators such as GRAF.
• Supports comparative studies of cellularization in animals and chytrid fungi, where mechanisms differ from conventional cytokinesis [4,8].
• Offers a model for studying membrane trafficking pathways during cell division.
• Enables quantitative measurements of contractile ring tension using laser ablation during Drosophila cellularization.
• Helps interpret developmental phenotypes caused by furrow gene mutations, including failed cell partitioning [5,6].
• Guides CRISPR-based functional studies of furrow components in model organisms [1,3,5].
Structure and Composition of cellularization cleavage furrow
Membrane invagination and furrow initiation
In simple terms: The furrow starts as an inward fold of the outer membrane that will eventually surround each nucleus.
The cellularization cleavage furrow is defined as a plasma membrane invagination at the site of separation of a multi-nucleate cell or syncytium into individual cells. In Drosophila embryos, furrows initiate at the cortex and invaginate around nuclei, forming a specialized membrane domain. The BAR domain protein amphiphysin is required for cleavage furrow tip-tubule formation during cellularization, indicating that membrane curvature generation is an early structural requirement. Membrane trafficking pathways also contribute to the membrane supply needed for furrow growth during cytokinesis-like events.
Actomyosin ring and contractile machinery
In simple terms: A ring of actin and myosin provides the force that helps the furrow move inward.
The furrow is associated with an actomyosin ring that generates contractile force. In Drosophila cellularization, the RhoGTPase protein GRAF is spatiotemporally recruited to inhibit actomyosin ring constriction, showing that ring activity is locally restrained. The early zygotic gene product Dunk interacts with anillin to regulate Myosin II during Drosophila cleavage, linking anillin and Myosin II to furrow function. Contractile ring tension can be measured directly using two-photon laser ablation during Drosophila cellularization, confirming that the ring is a mechanically active component of the furrow apparatus.
Slam and furrow stabilization
In simple terms: Slam is a protein that helps organize and stabilize the furrow as it forms.
Slam is a key furrow component in early Drosophila embryos. Studies of Slam function and dynamics in furrow formation show that it contributes to the organization of the furrow during cellularization. Together with actomyosin regulators and membrane-shaping proteins, Slam helps coordinate the structural integrity of the invagination as it extends around nuclei [1,6].
Membrane trafficking and tip tubules
In simple terms: Vesicles and tubules deliver membrane and proteins to the growing furrow.
Membrane trafficking is essential for furrow growth and maintenance. Pathways for membrane trafficking during cytokinesis provide a framework for understanding how vesicles supply membrane to the cleavage furrow. In Drosophila cellularization, amphiphysin-dependent tip-tubule formation at the cleavage furrow highlights a specialized membrane-remodeling step that supports furrow architecture. These trafficking and tubulation events distinguish cellularization cleavage furrows from simpler membrane invaginations.
Comparative structure in chytrid fungi
In simple terms: Some fungi build cellularization furrows using a different toolkit than animals.
Cellularization in chytrid fungi uses distinct mechanisms from conventional cytokinesis and from cellularization in animals and yeast [4,8]. This comparative finding indicates that the cellularization cleavage furrow, while defined by its membrane invagination function, can be assembled by divergent molecular components across lineages. Researchers can therefore use GO:0110070 to annotate furrow-like structures in diverse organisms while recognizing mechanistic differences [4,8].
Key Genes Involved in GO:0110070 cellularization cleavage furrow
The following genes and proteins have been experimentally linked to cellularization cleavage furrow structure, regulation, or function in the cited literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| amph | BAR domain protein required for cleavage furrow tip-tubule formation | Links membrane curvature to furrow architecture in Drosophila cellularization |
| GRAF | RhoGTPase regulator that inhibits actomyosin ring constriction | Provides spatiotemporal control of contractility during cellularization |
| Dunk | Early zygotic gene product that interacts with anillin to regulate Myosin II | Connects zygotic gene expression to furrow contractility |
| anillin | Actin-binding protein that interacts with Dunk and regulates Myosin II | Central scaffold for actomyosin organization at the furrow |
| slam | Furrow component involved in furrow formation and dynamics | Key marker and functional regulator of Drosophila cellularization |
| Myosin II | Motor protein that generates contractile force at the furrow | Target of regulation by Dunk, anillin, and GRAF [3,5] |
| Actin | Cytoskeletal filament that forms the actomyosin ring | Structural backbone of the contractile apparatus [3,7] |
| Rho GTPase | Signaling GTPase controlling actomyosin dynamics | Regulated by GRAF at the cellularization furrow |
| Amphiphysin | Membrane curvature protein with BAR domain | Required for tip-tubule formation at the furrow |
| Clathrin | Vesicle coat protein involved in membrane trafficking | Part of general trafficking pathways relevant to furrow membrane supply |
| Dynamin | GTPase involved in membrane fission | Relevant to membrane remodeling during cytokinesis-like events |
| Rab GTPases | Regulators of vesicle trafficking | Candidate components of furrow-directed membrane delivery |
| SNAREs | Membrane fusion machinery | Potential mediators of vesicle fusion at the furrow |
| Anillin | Scaffold linking actin and Myosin II | Functional partner of Dunk in furrow regulation |
| Slam | Membrane-associated furrow protein | Studied for dynamics during furrow formation |
| GRAF | RhoGAP-family regulator | Inhibits ring constriction in a spatiotemporal manner |
| Dunk | Zygotic factor regulating Myosin II | Connects early gene expression to furrow mechanics |
| Amphiphysin | BAR-domain membrane shaper | Required for furrow tip tubules |
How Is cellularization cleavage furrow Regulated?
Regulation of the cellularization cleavage furrow involves spatiotemporal control of actomyosin contractility and membrane remodeling. The RhoGTPase regulator GRAF is recruited to the furrow to inhibit actomyosin ring constriction, preventing premature or excessive contraction during Drosophila cellularization. Dunk, an early zygotic gene product, interacts with anillin to regulate Myosin II, linking developmental gene expression to furrow mechanics. Slam contributes to furrow formation and dynamics, further shaping the regulatory landscape. Membrane trafficking pathways also regulate furrow growth by controlling the delivery of membrane and proteins to the invagination site. Together, these mechanisms ensure that furrow assembly is coordinated with nuclear positioning and developmental timing [1,3,5,6].
cellularization cleavage furrow and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| amph | Failed furrow tip-tubule formation and cellularization defects | Drosophila knockout or point-mutation models |
| GRAF | Abnormal actomyosin ring constriction | Drosophila overexpression or knockout of GRAF |
| Dunk | Defective Myosin II regulation during cleavage | Drosophila zygotic mutant or knock-in tagging |
| anillin | Disrupted actomyosin organization at the furrow | Drosophila knockout and rescue models |
| slam | Impaired furrow formation and dynamics | Drosophila mutant and live-imaging models |
Developmental defects and failed cell partitioning
Disruption of cellularization cleavage furrow components can cause failed partitioning of syncytial cytoplasm into individual cells. In Drosophila, mutations affecting amphiphysin, Slam, anillin, Dunk, or Myosin II regulation lead to abnormal furrow formation and cellularization defects [1,3,5,6]. These phenotypes highlight how furrow dysfunction can disrupt tissue architecture during development. Because the furrow is a cellular component, its failure manifests as structural and morphogenetic defects rather than a specific metabolic disease [1,5,6].
Actomyosin contractility and cytoskeletal disease relevance
The furrow is an actomyosin-driven structure, and its regulators overlap with pathways implicated in cytoskeletal and contractility disorders. GRAF-mediated inhibition of actomyosin ring constriction demonstrates that Rho GTPase signaling must be tightly controlled at the furrow. Dunk and anillin regulate Myosin II, connecting furrow biology to the broader machinery of cell division and cytoskeletal organization. Studying these regulators can inform understanding of diseases where actomyosin dynamics are perturbed [3,5].
Comparative and evolutionary disease models
Chytrid fungi cellularize using mechanisms distinct from conventional cytokinesis and from animal cellularization, offering an evolutionary perspective on furrow biology [4,8]. This comparative context can help identify core versus lineage-specific furrow components. While direct human disease links for GO:0110070 are limited in the cited literature, the term provides a framework for studying cell partitioning defects in diverse organisms [4,8].
From cellularization cleavage furrow-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is a candidate gene required for furrow formation? | CRISPR knockout in Drosophila or chytrid fungi [1,4,5] |
| Does a specific residue control furrow protein function? | Point-mutation knock-in at the endogenous locus [1,3,5] |
| Where and when does a furrow protein localize? | Tagged knock-in with fluorescent protein |
| Does excess furrow protein alter contractility? | Overexpression of wild-type or mutant cDNA [3,5] |
| How does furrow tension change over time? | Two-photon laser ablation during cellularization |
| Are furrow mechanisms conserved across lineages? | Comparative cellularization assays in chytrid fungi and Drosophila [4,8] |
How to Study the cellularization cleavage furrow Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Live fluorescence imaging | Localization and dynamics of furrow proteins | Tracking Slam or tagged furrow components during cellularization |
| Two-photon laser ablation | Contractile ring tension | Quantifying furrow mechanics in Drosophila embryos |
| CRISPR knockout | Requirement of a gene for furrow formation | Testing amphiphysin, GRAF, Dunk, or anillin function [1,3,5] |
| Overexpression | Gain-of-function effects on furrow behavior | Assessing actomyosin ring regulation |
| Membrane trafficking assays | Vesicle and tubule contribution to furrow growth | Studying membrane supply during cellularization [1,2] |
| Comparative imaging | Conservation of furrow mechanisms | Analyzing chytrid fungal cellularization [4,8] |
| Phenotypic scoring | Cellularization success or failure | Evaluating developmental defects in mutants [1,5,6] |
| Protein interaction assays | Physical links between furrow components | Testing Dunk-anillin-Myosin II interactions |
Live imaging of furrow dynamics
Live imaging is a primary method for studying the cellularization cleavage furrow because the structure is dynamic and membrane-associated. Fluorescently tagged furrow proteins such as Slam can be tracked during Drosophila cellularization to reveal recruitment and dynamics. Two-photon laser ablation can measure contractile ring tension in living embryos, providing mechanical readouts of furrow function. These approaches are essential for linking molecular components to structural behavior [1,6,7].
Genetic perturbation and phenotypic analysis
Genetic perturbation is used to test whether specific genes are required for furrow formation. Knockout or mutation of amphiphysin, GRAF, Dunk, anillin, or Slam produces cellularization defects that can be scored by imaging [1,3,5,6]. Overexpression experiments can reveal gain-of-function effects on actomyosin ring behavior. These methods connect gene function to the cellular component GO:0110070 [1,3,5,6].
Membrane trafficking assays
Because furrow growth depends on membrane delivery, trafficking assays help define how vesicles and tubules contribute to the invagination. Pathways for membrane trafficking during cytokinesis provide a conceptual and experimental framework for these studies. In Drosophila, amphiphysin-dependent tip-tubule formation can be examined as a specialized trafficking-related event at the furrow. Such assays link membrane remodeling to furrow structure [1,2].
Comparative cellularization studies
Comparative studies in chytrid fungi reveal that cellularization can proceed through mechanisms distinct from conventional cytokinesis and animal cellularization [4,8]. These studies use genetic and imaging approaches to identify lineage-specific furrow components. They help determine which features of GO:0110070 are conserved and which are taxon-specific [4,8].
How CRISPR Can Be Used to Study GO:0110070 cellularization cleavage furrow
Knockout
CRISPR knockout is used to remove a candidate furrow gene and test whether cellularization cleavage furrow formation fails. For example, knocking out amphiphysin or GRAF in Drosophila can reveal requirements for tip-tubule formation or actomyosin ring regulation [1,3]. Knockout of Dunk or anillin can test their roles in Myosin II regulation during cleavage. These models directly connect gene loss to the cellular component GO:0110070 [1,3,5].
Point Mutation
Point-mutation models allow precise dissection of protein domains or residues that control furrow function. For instance, mutations in the BAR domain of amphiphysin can test its specific role in cleavage furrow tip-tubule formation. Point mutations in regulators such as GRAF can reveal how RhoGTPase signaling is tuned at the furrow. These models distinguish domain-specific functions from complete loss of protein [1,3].
Knock-in
Knock-in of fluorescent or epitope tags enables visualization of endogenous furrow proteins. Tagging Slam or other furrow components allows live tracking of their localization and dynamics during cellularization. Tagged knock-in of Dunk or anillin can reveal where these proteins act relative to the actomyosin ring. This approach preserves endogenous regulation while providing a readout of furrow structure [5,6].
Overexpression
Overexpression models test whether excess furrow protein alters contractility or membrane remodeling. Overexpressing GRAF or its variants can change actomyosin ring constriction during Drosophila cellularization. Overexpression of Myosin II regulators such as Dunk or anillin can reveal gain-of-function effects on furrow mechanics. These experiments complement loss-of-function studies to define the regulatory range of furrow components [3,5].
How EDITGENE Supports cellularization cleavage furrow Research
Researchers studying cellularization cleavage furrow-related genes often need to determine whether a candidate gene is causally involved in furrow assembly, regulation, or membrane remodeling. Establishing causality requires precise genetic models that can remove, modify, tag, or overexpress the gene of interest in a relevant organism such as Drosophila or chytrid fungi. EDITGENE provides end-to-end CRISPR services to generate these models and to support downstream screening and bioinformatic analysis.
Contact EDITGENE today to design your custom CRISPR model for cellularization cleavage furrow research.
Frequently Asked Questions About cellularization cleavage furrow
What is GO:0110070 cellularization cleavage furrow?
GO:0110070 is a Gene Ontology cellular component term defined as a plasma membrane invagination at the site of separation of a multi-nucleate cell or syncytium into individual cells. It describes the specialized furrow structure that partitions a syncytium into separate cells [1,4,6].
What genes are involved in cellularization cleavage furrow?
Genes and proteins experimentally linked to this structure include amphiphysin (amph), GRAF, Dunk, anillin, Slam, Myosin II, actin, and Rho GTPase [1,3,5,6].
What is the function of the cellularization cleavage furrow?
Its major function is to partition a multi-nucleate cell or syncytium into individual cells by inward membrane growth and actomyosin-driven remodeling [1,3,4,6].
How is the cellularization cleavage furrow different from a cytokinetic furrow?
Cellularization cleavage furrows form in a syncytial context around multiple nuclei and can use distinct mechanisms from conventional cytokinesis, as shown in chytrid fungi and Drosophila [4,8].
Which model organisms are used to study cellularization cleavage furrows?
Drosophila melanogaster embryos are a primary model, and chytrid fungi provide a comparative system with distinct cellularization mechanisms [1,3,4,6,8].
What role does amphiphysin play at the cellularization cleavage furrow?
The BAR domain of amphiphysin is required for cleavage furrow tip-tubule formation during cellularization in Drosophila embryos.
How is actomyosin contractility regulated during cellularization?
The RhoGTPase protein GRAF is spatiotemporally recruited to inhibit actomyosin ring constriction, while Dunk interacts with anillin to regulate Myosin II [3,5].
Can CRISPR be used to study cellularization cleavage furrow genes?
Yes. CRISPR knockout, point-mutation, knock-in, and overexpression models can test the function of furrow genes such as amphiphysin, GRAF, Dunk, anillin, and Slam [1,3,5,6].
What methods measure furrow tension?
Two-photon laser ablation during Drosophila cellularization can measure contractile ring tension.
Why is GO:0110070 important for developmental biology?
It defines the structural platform that converts a syncytium into individual cells, and its disruption causes cellularization defects and abnormal actomyosin regulation [1,3,5,6].
Conclusion
GO:0110070 cellularization cleavage furrow is a cellular component term that captures the membrane invagination responsible for partitioning a syncytium into individual cells. Research in Drosophila and chytrid fungi has identified key components including amphiphysin, GRAF, Dunk, anillin, Slam, and Myosin II, and has revealed tight spatiotemporal regulation of actomyosin contractility and membrane remodeling [1,3,4,5,6,8]. The term provides a precise annotation anchor for genes and structures involved in cellularization. For researchers, studying this term requires combining genetic perturbation with live imaging and mechanical measurements. CRISPR-based knockout, point-mutation, knock-in, and overexpression models, together with library screening and bioinformatics, offer a systematic path to dissect furrow biology and its broader implications for cell partitioning and development [1,3,5,7].
References
- 1. Su J et al.. 2013. The BAR domain of amphiphysin is required for cleavage furrow tip-tubule formation during cellularization in Drosophila embryos.. Mol Biol Cell 24(9):1444-53 PMID: 23447705
- 2. Strickland LI et al.. 2004. Pathways for membrane trafficking during cytokinesis.. Trends Cell Biol 14(3):115-8 PMID: 15055200
- 3. Sharma S et al.. 2021. Spatiotemporal recruitment of RhoGTPase protein GRAF inhibits actomyosin ring constriction in Drosophila cellularization.. Elife 10 PMID: 33835025
- 4. Medina EM et al.. 2025. Cellularization in chytrid fungi uses distinct mechanisms from conventional cytokinesis and cellularization in animals and yeast.. bioRxiv PMID: 40196661
- 5. Chen J et al.. 2023. Early zygotic gene product Dunk interacts with anillin to regulate Myosin II during Drosophila cleavage.. Mol Biol Cell 34(10):ar102 PMID: 37494082
- 6. Acharya S et al.. 2014. Function and dynamics of slam in furrow formation in early Drosophila embryo.. Dev Biol 386(2):371-84 PMID: 24368071
- 7. Sharma S et al.. 2022. Measurement of Contractile Ring Tension Using Two-photon Laser Ablation during Drosophila Cellularization.. Bio Protoc 12(6):e4362 PMID: 35434185
- 8. Medina EM et al.. 2026. Cellularization in chytrid fungi uses distinct mechanisms from conventional cytokinesis and cellularization in animals and yeast.. Curr Biol 36(2):338-354.e5 PMID: 41401808
