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• W2949207575 abstract "The association of molecules within membrane microdomains is critical for the intracellular organization of cells. During polarization of the C. elegans zygote, both polarity proteins and actomyosin regulators associate within dynamic membrane-associated foci. Recently, a novel class of asymmetric membrane-associated structures was described that appeared to be enriched in phosphatidylinositol 4,5-bisphosphate (PIP2), suggesting that PIP2 domains could constitute signaling hubs to promote cell polarization and actin nucleation. Here, we probe the nature of these domains using a variety of membrane- and actin cortex-associated probes. These data demonstrate that these domains are filopodia, which are stimulated transiently during polarity establishment and accumulate in the zygote anterior. 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 and that the PIP2 pool as revealed by PHPLCδ1 simply reflects plasma membrane localization. Given the ubiquity of 3D membrane structures in cells, including filopodia, microvilli and membrane folds, similar caveats are likely to apply to analysis of membrane-associated molecules in a broad range of systems." @default.
• W2949207575 created "2019-06-27" @default.
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• W2949207575 date "2019-01-01" @default.
• W2949207575 modified "2023-09-25" @default.
• W2949207575 title "Anterior-enriched filopodia create appearance of asymmetric membrane microdomains in polarizing<i>C. elegans</i>zygotes" @default.
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• W2949207575 doi "https://doi.org/10.1242/jcs.230714" @default.
• W2949207575 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6679585" @default.
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