Source 1primary paper2025MED
Toolkit/in vivo bimolecular fluorescence complementation
in vivo bimolecular fluorescence complementation
Also known as: BiFC
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Using in vivo bimolecular fluorescence complementation, we find that Wbm0152 interacts with the Vps2p subunit of the ESCRT-III subcomplex as well as the Vps2p ortholog (BmVps2, Bm6583b) from a Wolbachia host nematode, Brugia malayi.
Usefulness & Problems
Why this is useful
This assay is used here to test whether Wbm0152 interacts with candidate host proteins in vivo. The abstract reports interaction signals with yeast Vps2p and the Brugia malayi ortholog BmVps2.; detecting protein-protein interactions involving Wbm0152
Source:
This assay is used here to test whether Wbm0152 interacts with candidate host proteins in vivo. The abstract reports interaction signals with yeast Vps2p and the Brugia malayi ortholog BmVps2.
Source:
detecting protein-protein interactions involving Wbm0152
Problem solved
It provides mechanistic interaction evidence supporting the proposed link between Wbm0152 and ESCRT-III-associated factors.; provides interaction evidence linking Wbm0152 to Vps2-family ESCRT-III proteins
Source:
It provides mechanistic interaction evidence supporting the proposed link between Wbm0152 and ESCRT-III-associated factors.
Source:
provides interaction evidence linking Wbm0152 to Vps2-family ESCRT-III proteins
Problem links
provides interaction evidence linking Wbm0152 to Vps2-family ESCRT-III proteins
LiteratureIt provides mechanistic interaction evidence supporting the proposed link between Wbm0152 and ESCRT-III-associated factors.
Source:
It provides mechanistic interaction evidence supporting the proposed link between Wbm0152 and ESCRT-III-associated factors.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
bimolecular fluorescence complementationprotein-protein interaction-dependent fluorophore reconstitutionTechniques
Functional AssayTarget processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: sensor
It requires a bimolecular fluorescence complementation assay configuration in vivo with the proteins of interest.; requires a bimolecular fluorescence complementation setup with the proteins of interest
Independent follow-up evidence is still limited. Validation breadth across biological contexts is still narrow. Independent reuse still looks limited, so the evidence base may be fragile. No canonical validation observations are stored yet, so context-specific performance remains under-specified.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Wbm0152 expression strongly disrupts endosomal maturation and causes defects in ubiquitylated protein turnover.
Wbm0152 expression strongly disrupts endosomal maturation, leading to defects in ubiquitylated protein turnover.
Expression of Wbm0152 in Saccharomyces cerevisiae inhibits ESCRT complex activity.
In this work, we show that the expression of a Wolbachia outer membrane lipoprotein, wBm0152, in Saccharomyces cerevisiae inhibits the activity of the Endosomal Sorting Complex Required for Transport (ESCRT)
In vivo bimolecular fluorescence complementation detected interaction between Wbm0152 and the Brugia malayi Vps2 ortholog BmVps2.
Using in vivo bimolecular fluorescence complementation, we find that Wbm0152 interacts with ... the Vps2p ortholog (BmVps2, Bm6583b) from a Wolbachia host nematode, Brugia malayi.
In vivo bimolecular fluorescence complementation detected interaction between Wbm0152 and yeast Vps2p.
Using in vivo bimolecular fluorescence complementation, we find that Wbm0152 interacts with the Vps2p subunit of the ESCRT-III subcomplex
Approval Evidence
1 source2 linked approval claimsfirst-pass slug in-vivo-bimolecular-fluorescence-complementation
Using in vivo bimolecular fluorescence complementation, we find that Wbm0152 interacts with the Vps2p subunit of the ESCRT-III subcomplex as well as the Vps2p ortholog (BmVps2, Bm6583b) from a Wolbachia host nematode, Brugia malayi.
Source:
protein interactionsupports
In vivo bimolecular fluorescence complementation detected interaction between Wbm0152 and the Brugia malayi Vps2 ortholog BmVps2.
Using in vivo bimolecular fluorescence complementation, we find that Wbm0152 interacts with ... the Vps2p ortholog (BmVps2, Bm6583b) from a Wolbachia host nematode, Brugia malayi.
Source:
protein interactionsupports
In vivo bimolecular fluorescence complementation detected interaction between Wbm0152 and yeast Vps2p.
Using in vivo bimolecular fluorescence complementation, we find that Wbm0152 interacts with the Vps2p subunit of the ESCRT-III subcomplex
Source:
Comparisons
Source-backed strengths
identified interaction with both yeast Vps2p and Brugia malayi BmVps2
Source:
identified interaction with both yeast Vps2p and Brugia malayi BmVps2
Compared with Langendorff perfused heart electrical recordings
in vivo bimolecular fluorescence complementation and Langendorff perfused heart electrical recordings address a similar problem space.
Shared frame: same top-level item type
Strengths here: looks easier to implement in practice.
Compared with native green gel system
in vivo bimolecular fluorescence complementation and native green gel system address a similar problem space.
Shared frame: same top-level item type
Strengths here: looks easier to implement in practice.
in vivo bimolecular fluorescence complementation and sub-picosecond pump-probe analysis of bacteriorhodopsin pigments address a similar problem space.
Shared frame: same top-level item type
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.