Source 1primary paper2020
Toolkit/tau polyproline rich domain
tau polyproline rich domain
Also known as: polyproline rich domain, PRD
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The tau polyproline-rich domain (PRD) is a tau-derived protein domain that promotes liquid-liquid phase separation in cells. Available evidence indicates that its condensate-forming activity is regulated by phosphorylation and that, in the absence of the microtubule-binding domain, it can co-condense with EB1.
Usefulness & Problems
Why this is useful
This domain is useful as a genetically encoded module for studying how a defined region of tau contributes to intracellular liquid-liquid phase separation. It also provides a system for probing phosphorylation-dependent control of condensate behavior and the relationship between tau domain architecture and EB1-associated co-condensation.
Source:
The specific domain properties of the MTBD and PRD serve distinct but mutually complementary roles that utilize LLPS in a cellular context
Problem solved
The PRD helps isolate the specific contribution of tau's polyproline-rich region to phase separation in a cellular context. It addresses the problem of disentangling the distinct but complementary roles of the polyproline-rich domain and the microtubule-binding domain in tau condensate biology.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
co-condensation with eb1liquid-liquid phase separationphosphorylation-dependent regulationTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Implementation Constraints
This tool is a protein domain derived from tau and has been studied in a cellular context. Practical details such as construct boundaries, expression system, delivery method, and any required design features are not specified in the supplied evidence, although interpretation should consider the presence or absence of the microtubule-binding domain and phosphorylation state.
The evidence base provided here comes from a single 2020 study, with no independent replication indicated. Quantitative performance characteristics, sequence boundaries, and validation across organisms, cell types, or assay formats are not provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The tau polyproline rich domain promotes liquid-liquid phase separation in cells.
The polyproline rich domain (PRD) drives LLPS
The tau polyproline rich domain promotes liquid-liquid phase separation in cells.
The polyproline rich domain (PRD) drives LLPS
The tau polyproline rich domain promotes liquid-liquid phase separation in cells.
The polyproline rich domain (PRD) drives LLPS
The tau polyproline rich domain promotes liquid-liquid phase separation in cells.
The polyproline rich domain (PRD) drives LLPS
The tau polyproline rich domain promotes liquid-liquid phase separation in cells.
The polyproline rich domain (PRD) drives LLPS
The tau polyproline rich domain promotes liquid-liquid phase separation in cells.
The polyproline rich domain (PRD) drives LLPS
The tau polyproline rich domain promotes liquid-liquid phase separation in cells.
The polyproline rich domain (PRD) drives LLPS
The microtubule-binding domain and polyproline rich domain of tau have distinct but complementary roles that utilize liquid-liquid phase separation in a cellular context.
The specific domain properties of the MTBD and PRD serve distinct but mutually complementary roles that utilize LLPS in a cellular context
The microtubule-binding domain and polyproline rich domain of tau have distinct but complementary roles that utilize liquid-liquid phase separation in a cellular context.
The specific domain properties of the MTBD and PRD serve distinct but mutually complementary roles that utilize LLPS in a cellular context
The microtubule-binding domain and polyproline rich domain of tau have distinct but complementary roles that utilize liquid-liquid phase separation in a cellular context.
The specific domain properties of the MTBD and PRD serve distinct but mutually complementary roles that utilize LLPS in a cellular context
The microtubule-binding domain and polyproline rich domain of tau have distinct but complementary roles that utilize liquid-liquid phase separation in a cellular context.
The specific domain properties of the MTBD and PRD serve distinct but mutually complementary roles that utilize LLPS in a cellular context
The microtubule-binding domain and polyproline rich domain of tau have distinct but complementary roles that utilize liquid-liquid phase separation in a cellular context.
The specific domain properties of the MTBD and PRD serve distinct but mutually complementary roles that utilize LLPS in a cellular context
The microtubule-binding domain and polyproline rich domain of tau have distinct but complementary roles that utilize liquid-liquid phase separation in a cellular context.
The specific domain properties of the MTBD and PRD serve distinct but mutually complementary roles that utilize LLPS in a cellular context
The microtubule-binding domain and polyproline rich domain of tau have distinct but complementary roles that utilize liquid-liquid phase separation in a cellular context.
The specific domain properties of the MTBD and PRD serve distinct but mutually complementary roles that utilize LLPS in a cellular context
In the absence of the microtubule-binding domain, the tau polyproline rich domain co-condenses with EB1.
In absence of the MTBD, the tau PRD co-condensed with EB1
In the absence of the microtubule-binding domain, the tau polyproline rich domain co-condenses with EB1.
In absence of the MTBD, the tau PRD co-condensed with EB1
In the absence of the microtubule-binding domain, the tau polyproline rich domain co-condenses with EB1.
In absence of the MTBD, the tau PRD co-condensed with EB1
In the absence of the microtubule-binding domain, the tau polyproline rich domain co-condenses with EB1.
In absence of the MTBD, the tau PRD co-condensed with EB1
In the absence of the microtubule-binding domain, the tau polyproline rich domain co-condenses with EB1.
In absence of the MTBD, the tau PRD co-condensed with EB1
In the absence of the microtubule-binding domain, the tau polyproline rich domain co-condenses with EB1.
In absence of the MTBD, the tau PRD co-condensed with EB1
In the absence of the microtubule-binding domain, the tau polyproline rich domain co-condenses with EB1.
In absence of the MTBD, the tau PRD co-condensed with EB1
The tau polyproline rich domain drives liquid-liquid phase separation under the control of phosphorylation.
The polyproline rich domain (PRD) drives LLPS and does so under the control of phosphorylation.
The tau polyproline rich domain drives liquid-liquid phase separation under the control of phosphorylation.
The polyproline rich domain (PRD) drives LLPS and does so under the control of phosphorylation.
The tau polyproline rich domain drives liquid-liquid phase separation under the control of phosphorylation.
The polyproline rich domain (PRD) drives LLPS and does so under the control of phosphorylation.
The tau polyproline rich domain drives liquid-liquid phase separation under the control of phosphorylation.
The polyproline rich domain (PRD) drives LLPS and does so under the control of phosphorylation.
The tau polyproline rich domain drives liquid-liquid phase separation under the control of phosphorylation.
The polyproline rich domain (PRD) drives LLPS and does so under the control of phosphorylation.
The tau polyproline rich domain drives liquid-liquid phase separation under the control of phosphorylation.
The polyproline rich domain (PRD) drives LLPS and does so under the control of phosphorylation.
The tau polyproline rich domain drives liquid-liquid phase separation under the control of phosphorylation.
The polyproline rich domain (PRD) drives LLPS and does so under the control of phosphorylation.
Approval Evidence
1 source4 linked approval claimsfirst-pass slug tau-polyproline-rich-domain
The polyproline rich domain (PRD) drives LLPS and does so under the control of phosphorylation.
Source:
activitysupports
The tau polyproline rich domain promotes liquid-liquid phase separation in cells.
The polyproline rich domain (PRD) drives LLPS
Source:
functional rolesupports
The microtubule-binding domain and polyproline rich domain of tau have distinct but complementary roles that utilize liquid-liquid phase separation in a cellular context.
The specific domain properties of the MTBD and PRD serve distinct but mutually complementary roles that utilize LLPS in a cellular context
Source:
interactionsupports
In the absence of the microtubule-binding domain, the tau polyproline rich domain co-condenses with EB1.
In absence of the MTBD, the tau PRD co-condensed with EB1
Source:
regulationsupports
The tau polyproline rich domain drives liquid-liquid phase separation under the control of phosphorylation.
The polyproline rich domain (PRD) drives LLPS and does so under the control of phosphorylation.
Source:
Comparisons
Source-backed strengths
Evidence from the cited study supports that the PRD alone can drive liquid-liquid phase separation in cells. The same source indicates regulatory control by phosphorylation and a specific interaction phenotype, co-condensation with EB1 when the microtubule-binding domain is absent.
Ranked Citations
- 1.