Source 1primary paper2019Journal of Cell Science
Toolkit/PHPLCδ1
PHPLCδ1
Also known as: PHPLCb41
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
PHPLCδ1 is a phosphoinositide-binding pleckstrin homology domain used as a membrane-associated fluorescence probe. In the cited 2019 C. elegans zygote study, its reported PIP2 signal was interpreted as reflecting general plasma membrane localization rather than selective enrichment in a distinct PIP2 microdomain.
Usefulness & Problems
Why this is useful
PHPLCδ1 is useful as a reporter for membrane-associated PIP2-linked fluorescence localization in live-cell imaging contexts. The supplied evidence specifically supports its use for interpreting whether apparent cortical signal asymmetries track plasma membrane topology in polarizing C. elegans zygotes.
Problem solved
This probe helps distinguish apparent phosphoinositide-associated fluorescence enrichment from signal changes caused by plasma membrane geometry. In the cited system, it addressed whether anterior cortical signal represented a bona fide PIP2 microdomain or simply membrane-localized signal on filopodial protrusions.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
Selection / EnrichmentTarget processes
localizationrecombinationselectionImplementation Constraints
The evidence indicates use as a membrane-associated fluorescence probe in a C. elegans zygote imaging study. No additional construct architecture, fluorophore choice, expression strategy, or cofactor requirements are provided in the supplied evidence.
The supplied evidence is limited to one interpretation study in C. elegans zygotes and does not provide quantitative binding properties, specificity measurements, or cross-system validation. In this context, PHPLCδ1 did not resolve a distinct PIP2 microdomain, because its reported signal was interpreted as general plasma membrane localization.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Local increases in fluorescence signal of membrane-associated molecules in the anterior-enriched domains can be quantitatively explained by membrane protrusion topology rather than selective molecular enrichment relative to bulk membrane.
The resulting membrane protrusions create local membrane topology that quantitatively accounts for observed local increases in the fluorescence signal of membrane-associated molecules, suggesting molecules are not selectively enriched in these domains relative to bulk membrane
Local increases in fluorescence signal of membrane-associated molecules in the anterior-enriched domains can be quantitatively explained by membrane protrusion topology rather than selective molecular enrichment relative to bulk membrane.
The resulting membrane protrusions create local membrane topology that quantitatively accounts for observed local increases in the fluorescence signal of membrane-associated molecules, suggesting molecules are not selectively enriched in these domains relative to bulk membrane
Local increases in fluorescence signal of membrane-associated molecules in the anterior-enriched domains can be quantitatively explained by membrane protrusion topology rather than selective molecular enrichment relative to bulk membrane.
The resulting membrane protrusions create local membrane topology that quantitatively accounts for observed local increases in the fluorescence signal of membrane-associated molecules, suggesting molecules are not selectively enriched in these domains relative to bulk membrane
Local increases in fluorescence signal of membrane-associated molecules in the anterior-enriched domains can be quantitatively explained by membrane protrusion topology rather than selective molecular enrichment relative to bulk membrane.
The resulting membrane protrusions create local membrane topology that quantitatively accounts for observed local increases in the fluorescence signal of membrane-associated molecules, suggesting molecules are not selectively enriched in these domains relative to bulk membrane
Local increases in fluorescence signal of membrane-associated molecules in the anterior-enriched domains can be quantitatively explained by membrane protrusion topology rather than selective molecular enrichment relative to bulk membrane.
The resulting membrane protrusions create local membrane topology that quantitatively accounts for observed local increases in the fluorescence signal of membrane-associated molecules, suggesting molecules are not selectively enriched in these domains relative to bulk membrane
Local increases in fluorescence signal of membrane-associated molecules in the anterior-enriched domains can be quantitatively explained by membrane protrusion topology rather than selective molecular enrichment relative to bulk membrane.
The resulting membrane protrusions create local membrane topology that quantitatively accounts for observed local increases in the fluorescence signal of membrane-associated molecules, suggesting molecules are not selectively enriched in these domains relative to bulk membrane
Local increases in fluorescence signal of membrane-associated molecules in the anterior-enriched domains can be quantitatively explained by membrane protrusion topology rather than selective molecular enrichment relative to bulk membrane.
The resulting membrane protrusions create local membrane topology that quantitatively accounts for observed local increases in the fluorescence signal of membrane-associated molecules, suggesting molecules are not selectively enriched in these domains relative to bulk membrane
The asymmetric membrane-associated structures observed during polarization of the C. elegans zygote are filopodia.
These data demonstrate that these domains are filopodia
The asymmetric membrane-associated structures observed during polarization of the C. elegans zygote are filopodia.
These data demonstrate that these domains are filopodia
The asymmetric membrane-associated structures observed during polarization of the C. elegans zygote are filopodia.
These data demonstrate that these domains are filopodia
The asymmetric membrane-associated structures observed during polarization of the C. elegans zygote are filopodia.
These data demonstrate that these domains are filopodia
The asymmetric membrane-associated structures observed during polarization of the C. elegans zygote are filopodia.
These data demonstrate that these domains are filopodia
The asymmetric membrane-associated structures observed during polarization of the C. elegans zygote are filopodia.
These data demonstrate that these domains are filopodia
The asymmetric membrane-associated structures observed during polarization of the C. elegans zygote are filopodia.
These data demonstrate that these domains are filopodia
The PIP2 pool reported by PHPLCδ1 in these domains reflects plasma membrane localization rather than selective enrichment in a distinct PIP2 microdomain.
the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization
The PIP2 pool reported by PHPLCδ1 in these domains reflects plasma membrane localization rather than selective enrichment in a distinct PIP2 microdomain.
the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization
The PIP2 pool reported by PHPLCδ1 in these domains reflects plasma membrane localization rather than selective enrichment in a distinct PIP2 microdomain.
the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization
The PIP2 pool reported by PHPLCδ1 in these domains reflects plasma membrane localization rather than selective enrichment in a distinct PIP2 microdomain.
the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization
The PIP2 pool reported by PHPLCδ1 in these domains reflects plasma membrane localization rather than selective enrichment in a distinct PIP2 microdomain.
the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization
The PIP2 pool reported by PHPLCδ1 in these domains reflects plasma membrane localization rather than selective enrichment in a distinct PIP2 microdomain.
the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization
The PIP2 pool reported by PHPLCδ1 in these domains reflects plasma membrane localization rather than selective enrichment in a distinct PIP2 microdomain.
the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization
Approval Evidence
1 source3 linked approval claimsfirst-pass slug phplc-1
the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization
Source:
localization interpretationsupports
Local increases in fluorescence signal of membrane-associated molecules in the anterior-enriched domains can be quantitatively explained by membrane protrusion topology rather than selective molecular enrichment relative to bulk membrane.
The resulting membrane protrusions create local membrane topology that quantitatively accounts for observed local increases in the fluorescence signal of membrane-associated molecules, suggesting molecules are not selectively enriched in these domains relative to bulk membrane
Source:
mechanistic identitysupports
The asymmetric membrane-associated structures observed during polarization of the C. elegans zygote are filopodia.
These data demonstrate that these domains are filopodia
Source:
probe interpretationsupports
The PIP2 pool reported by PHPLCδ1 in these domains reflects plasma membrane localization rather than selective enrichment in a distinct PIP2 microdomain.
the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization
Source:
Comparisons
Source-backed strengths
The cited study supports PHPLCδ1 as an informative reporter for plasma membrane-associated PIP2 signal during C. elegans zygote polarization. Its signal contributed to the conclusion that anterior-enriched fluorescence could be explained by filopodial membrane topology rather than selective molecular enrichment.
Ranked Citations
- 1.