Toolkit/defined oligomers of CENP-T

defined oligomers of CENP-T

Multi-Component Switch·Research·Since 2023

Also known as: defined oligomers of the inner kinetochore protein CENP-T, oligomerized CENP-T

Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.

Summary

Defined oligomers of CENP-T are genetically engineered multimeric assemblies of the inner kinetochore protein CENP-T produced using two distinct systems in human cells. These higher-order CENP-T assemblies increase recruitment of outer kinetochore components and, when configured to mimic centromeric density, can induce functional cytoplasmic kinetochore-like particles.

Usefulness & Problems

Why this is useful

This tool is useful for experimentally controlling CENP-T higher-order assembly to probe how inner kinetochore organization regulates outer kinetochore recruitment. It provides a way to test whether CENP-T density and oligomeric state are sufficient to drive kinetochore-like assembly outside the native centromere context.

Source:

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles

Problem solved

It addresses the problem of dissecting how higher-order assembly of an inner kinetochore component contributes to outer kinetochore recruitment. Specifically, it enables direct comparison of oligomerized versus monomeric CENP-T in human cells and tests whether centromere-like CENP-T density can trigger functional kinetochore-like particle formation.

Problem links

Need inducible protein relocalization or recruitment

Derived

Defined oligomers of the inner kinetochore protein CENP-T are genetically engineered multimeric CENP-T assemblies generated using two distinct systems in human cells. These oligomers act as a higher-order assembly switch that promotes recruitment of outer kinetochore components and can induce functional cytoplasmic kinetochore-like particles when CENP-T density mimics centromeric conditions.

Taxonomy & Function

Primary hierarchy

Mechanism Branch

Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.

Techniques

No technique tags yet.

Target processes

localization

Implementation Constraints

cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: actuatoroperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment

Defined oligomers were generated using two distinct genetically engineered systems in human cells. The evidence indicates that functional cytoplasmic kinetochore-like particle formation depends on achieving CENP-T oligomer states that mimic centromeric density, but construct architecture and delivery details are not described in the supplied material.

The available evidence is limited to a single 2023 source and does not specify the exact oligomerization systems, stoichiometries, or the full set of recruited outer kinetochore components. Evidence for performance across other cell types, organisms, or experimental contexts is not provided.

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Observations

successMammalian Cell Lineapplication demohuman

Inferred from claim c3 during normalization. CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles. Derived from claim c3. Quoted text: oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles

Source:

successMammalian Cell Lineapplication demohuman

Inferred from claim c3 during normalization. CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles. Derived from claim c3. Quoted text: oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles

Source:

successMammalian Cell Lineapplication demohuman

Inferred from claim c3 during normalization. CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles. Derived from claim c3. Quoted text: oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles

Source:

successMammalian Cell Lineapplication demohuman

Inferred from claim c3 during normalization. CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles. Derived from claim c3. Quoted text: oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles

Source:

successMammalian Cell Lineapplication demohuman

Inferred from claim c3 during normalization. CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles. Derived from claim c3. Quoted text: oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles

Source:

successMammalian Cell Lineapplication demohuman

Inferred from claim c3 during normalization. CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles. Derived from claim c3. Quoted text: oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles

Source:

successMammalian Cell Lineapplication demohuman

Inferred from claim c3 during normalization. CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles. Derived from claim c3. Quoted text: oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles

Source:

Supporting Sources

Ranked Claims

Claim 1comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 2comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 3comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 4comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 5comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 6comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 7comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 8comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 9comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 10comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 11comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 12comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 13comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 14comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 15comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 16comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 17comparative activitysupports2023Source 1needs review

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.
Claim 18functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 19functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 20functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 21functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 22functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 23functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 24functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 25functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 26functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 27functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 28functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 29functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 30functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 31functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 32functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 33functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 34functional effectsupports2023Source 1needs review

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles
Claim 35mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 36mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 37mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 38mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 39mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 40mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 41mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 42mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 43mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 44mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 45mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 46mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 47mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 48mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 49mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 50mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 51mechanismsupports2023Source 1needs review

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Claim 52regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 53regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 54regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 55regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 56regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 57regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 58regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 59regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 60regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 61regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 62regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 63regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 64regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 65regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 66regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 67regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.
Claim 68regulatory modelsupports2023Source 1needs review

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.

Approval Evidence

1 source4 linked approval claimsfirst-pass slug defined-oligomers-of-cenp-t
we generated defined oligomers of the inner kinetochore protein CENP-T using two distinct, genetically engineered systems in human cells

Source:

comparative activitysupports

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T.

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.

Source:

functional effectsupports

CENP-T oligomers that mimic centromeric density trigger formation of functional cytoplasmic kinetochore-like particles.

oligomers that mimic the centromeric density of CENP-T trigger the robust formation of functional, cytoplasmic kinetochore-like particles

Source:

mechanismsupports

Higher-order assembly of CENP-T promotes outer kinetochore recruitment.

Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment

Source:

regulatory modelsupports

Density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres.

Thus, the density-dependence of CENP-T restricts outer kinetochore recruitment to centromeres, where densely packed CENP-A recruits a high local concentration of CENP-T.

Source:

Comparisons

Source-backed strengths

Oligomerized CENP-T recruits higher levels of outer kinetochore components than monomeric CENP-T, supporting a clear activity difference linked to assembly state. The tool was implemented with two distinct genetically engineered systems in human cells, and CENP-T oligomers that mimic centromeric density were reported to generate functional cytoplasmic kinetochore-like particles.

Source:

Both in cells and in vitro , each molecule of oligomerized CENP-T recruits substantially higher levels of outer kinetochore components than monomeric CENP-T molecules.

Compared with Cry2

defined oligomers of CENP-T and Cry2 address a similar problem space because they share localization.

Shared frame: same top-level item type; shared target processes: localization; shared mechanisms: oligomerization

Strengths here: looks easier to implement in practice; may avoid an exogenous cofactor requirement.

Relative tradeoffs: appears more independently replicated.

Compared with CRY2/CIB1

defined oligomers of CENP-T and CRY2/CIB1 address a similar problem space because they share localization.

Shared frame: same top-level item type; shared target processes: localization; shared mechanisms: oligomerization

Relative tradeoffs: appears more independently replicated.

Compared with synthetic condensates

defined oligomers of CENP-T and synthetic condensates address a similar problem space because they share localization.

Shared frame: same top-level item type; shared target processes: localization; shared mechanisms: oligomerization

Ranked Citations

  1. 1.
    StructuralSource 12023Claim 17Claim 16Claim 16

    Extracted from this source document.