Source 1primary paper2020
Toolkit/SMN tudor domain
SMN tudor domain
Also known as: SMN's globular tudor domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The SMN tudor domain is a globular protein domain from SMN that is sufficient for dimerization-induced condensation in vivo. Its condensate-forming activity requires binding to dimethylarginine, supporting its use as a chemical-input interaction module for specifying membraneless organelle assembly.
Usefulness & Problems
Why this is useful
This domain is useful as a compact protein module for coupling dimethylarginine recognition to condensate formation in living cells. The cited study further indicates that DMA-tudor interaction modules can regulate membraneless organelle assembly and define condensate composition.
Problem solved
The SMN tudor domain helps address the problem of how to encode chemically specified assembly of intracellular condensates using a defined protein interaction module. It provides a way to link dimethylarginine-dependent molecular recognition to dimerization-induced condensation in vivo.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Chemical
Implementation Constraints
Implementation appears to rely on the isolated SMN globular tudor domain and on dimerization-induced condensation in vivo. Practical use is expected to require access to dimethylarginine-dependent binding partners or contexts in which dimethylarginine recognition can occur, but the supplied evidence does not detail construct design beyond domain sufficiency.
The available evidence is limited to a single cited study and does not provide quantitative performance metrics, construct architectures, or cross-system benchmarking. The current evidence also does not specify host organisms, expression conditions, or the extent of validation beyond in vivo condensation assays.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The condensate-forming property associated with the SMN tudor domain is shared by at least seven additional tudor domains in six different proteins.
was shared by at least seven additional tudor domains in six different proteins
additional tudor domains 7different proteins 6
The condensate-forming property associated with the SMN tudor domain is shared by at least seven additional tudor domains in six different proteins.
was shared by at least seven additional tudor domains in six different proteins
additional tudor domains 7different proteins 6
The condensate-forming property associated with the SMN tudor domain is shared by at least seven additional tudor domains in six different proteins.
was shared by at least seven additional tudor domains in six different proteins
additional tudor domains 7different proteins 6
The condensate-forming property associated with the SMN tudor domain is shared by at least seven additional tudor domains in six different proteins.
was shared by at least seven additional tudor domains in six different proteins
additional tudor domains 7different proteins 6
The condensate-forming property associated with the SMN tudor domain is shared by at least seven additional tudor domains in six different proteins.
was shared by at least seven additional tudor domains in six different proteins
additional tudor domains 7different proteins 6
The condensate-forming property associated with the SMN tudor domain is shared by at least seven additional tudor domains in six different proteins.
was shared by at least seven additional tudor domains in six different proteins
additional tudor domains 7different proteins 6
The condensate-forming property associated with the SMN tudor domain is shared by at least seven additional tudor domains in six different proteins.
was shared by at least seven additional tudor domains in six different proteins
additional tudor domains 7different proteins 6
A tudor domain bound to dimethylarginine constitutes a versatile yet specific interaction module that regulates membraneless organelle assembly and defines composition.
the combination of a tudor domain bound to its DMA ligand – DMA-tudor – represents a versatile yet specific interaction module that regulates MLO assembly and defines their composition
A tudor domain bound to dimethylarginine constitutes a versatile yet specific interaction module that regulates membraneless organelle assembly and defines composition.
the combination of a tudor domain bound to its DMA ligand – DMA-tudor – represents a versatile yet specific interaction module that regulates MLO assembly and defines their composition
A tudor domain bound to dimethylarginine constitutes a versatile yet specific interaction module that regulates membraneless organelle assembly and defines composition.
the combination of a tudor domain bound to its DMA ligand – DMA-tudor – represents a versatile yet specific interaction module that regulates MLO assembly and defines their composition
A tudor domain bound to dimethylarginine constitutes a versatile yet specific interaction module that regulates membraneless organelle assembly and defines composition.
the combination of a tudor domain bound to its DMA ligand – DMA-tudor – represents a versatile yet specific interaction module that regulates MLO assembly and defines their composition
A tudor domain bound to dimethylarginine constitutes a versatile yet specific interaction module that regulates membraneless organelle assembly and defines composition.
the combination of a tudor domain bound to its DMA ligand – DMA-tudor – represents a versatile yet specific interaction module that regulates MLO assembly and defines their composition
A tudor domain bound to dimethylarginine constitutes a versatile yet specific interaction module that regulates membraneless organelle assembly and defines composition.
the combination of a tudor domain bound to its DMA ligand – DMA-tudor – represents a versatile yet specific interaction module that regulates MLO assembly and defines their composition
A tudor domain bound to dimethylarginine constitutes a versatile yet specific interaction module that regulates membraneless organelle assembly and defines composition.
the combination of a tudor domain bound to its DMA ligand – DMA-tudor – represents a versatile yet specific interaction module that regulates MLO assembly and defines their composition
The condensate-forming property of the SMN tudor domain requires binding to dimethylarginine.
The condensate-forming property of the SMN tudor domain required binding to its ligand, dimethylarginine (DMA)
The condensate-forming property of the SMN tudor domain requires binding to dimethylarginine.
The condensate-forming property of the SMN tudor domain required binding to its ligand, dimethylarginine (DMA)
The condensate-forming property of the SMN tudor domain requires binding to dimethylarginine.
The condensate-forming property of the SMN tudor domain required binding to its ligand, dimethylarginine (DMA)
The condensate-forming property of the SMN tudor domain requires binding to dimethylarginine.
The condensate-forming property of the SMN tudor domain required binding to its ligand, dimethylarginine (DMA)
The condensate-forming property of the SMN tudor domain requires binding to dimethylarginine.
The condensate-forming property of the SMN tudor domain required binding to its ligand, dimethylarginine (DMA)
The condensate-forming property of the SMN tudor domain requires binding to dimethylarginine.
The condensate-forming property of the SMN tudor domain required binding to its ligand, dimethylarginine (DMA)
The condensate-forming property of the SMN tudor domain requires binding to dimethylarginine.
The condensate-forming property of the SMN tudor domain required binding to its ligand, dimethylarginine (DMA)
Asymmetric versus symmetric dimethylarginine determines whether gems and Cajal bodies are separate or overlapping.
asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs – gems and Cajal bodies – were separate or overlapping
Asymmetric versus symmetric dimethylarginine determines whether gems and Cajal bodies are separate or overlapping.
asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs – gems and Cajal bodies – were separate or overlapping
Asymmetric versus symmetric dimethylarginine determines whether gems and Cajal bodies are separate or overlapping.
asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs – gems and Cajal bodies – were separate or overlapping
Asymmetric versus symmetric dimethylarginine determines whether gems and Cajal bodies are separate or overlapping.
asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs – gems and Cajal bodies – were separate or overlapping
Asymmetric versus symmetric dimethylarginine determines whether gems and Cajal bodies are separate or overlapping.
asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs – gems and Cajal bodies – were separate or overlapping
Asymmetric versus symmetric dimethylarginine determines whether gems and Cajal bodies are separate or overlapping.
asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs – gems and Cajal bodies – were separate or overlapping
Asymmetric versus symmetric dimethylarginine determines whether gems and Cajal bodies are separate or overlapping.
asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs – gems and Cajal bodies – were separate or overlapping
The SMN tudor domain is sufficient for dimerization-induced condensation in vivo.
SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo
The SMN tudor domain is sufficient for dimerization-induced condensation in vivo.
SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo
The SMN tudor domain is sufficient for dimerization-induced condensation in vivo.
SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo
The SMN tudor domain is sufficient for dimerization-induced condensation in vivo.
SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo
The SMN tudor domain is sufficient for dimerization-induced condensation in vivo.
SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo
The SMN tudor domain is sufficient for dimerization-induced condensation in vivo.
SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo
The SMN tudor domain is sufficient for dimerization-induced condensation in vivo.
SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo
Approval Evidence
1 source3 linked approval claimsfirst-pass slug smn-tudor-domain
SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo
Source:
generalizabilitysupports
The condensate-forming property associated with the SMN tudor domain is shared by at least seven additional tudor domains in six different proteins.
was shared by at least seven additional tudor domains in six different proteins
Source:
requirementsupports
The condensate-forming property of the SMN tudor domain requires binding to dimethylarginine.
The condensate-forming property of the SMN tudor domain required binding to its ligand, dimethylarginine (DMA)
Source:
sufficiencysupports
The SMN tudor domain is sufficient for dimerization-induced condensation in vivo.
SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo
Source:
Comparisons
Source-backed strengths
The domain was reported to be sufficient for dimerization-induced condensation in vivo, indicating that the globular tudor domain alone can confer this behavior. The underlying interaction logic is supported by evidence that condensate formation requires dimethylarginine binding, and related condensate-forming behavior was observed for at least seven additional tudor domains in six proteins.
Ranked Citations
- 1.