Source 1primary paper2023
Toolkit/defined oligomers of CENP-T
defined oligomers of CENP-T
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.
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
localizationImplementation Constraints
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
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.
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.
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.
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.
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.
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.
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.
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
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
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
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
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
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
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
Higher-order assembly of CENP-T promotes outer kinetochore recruitment.
Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Higher-order assembly of CENP-T promotes outer kinetochore recruitment.
Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Higher-order assembly of CENP-T promotes outer kinetochore recruitment.
Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Higher-order assembly of CENP-T promotes outer kinetochore recruitment.
Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Higher-order assembly of CENP-T promotes outer kinetochore recruitment.
Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Higher-order assembly of CENP-T promotes outer kinetochore recruitment.
Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
Higher-order assembly of CENP-T promotes outer kinetochore recruitment.
Higher-order assembly is a regulatory switch that promotes outer kinetochore recruitment
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.
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.
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.
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.
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.
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.
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.
Ranked Citations
- 1.