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PI(4,5)P2 forms dynamic cortical structures and directs actin distribution as well as polarity in C. elegans embryos
Author(s) -
Melina J. Scholze,
Kévin Barbieux,
Alessandro De Simone,
Mathilde Boumasmoud,
Camille C. N. Süess,
Ruijia Wang,
Pierre Gönczy
Publication year - 2018
Publication title -
development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.754
H-Index - 325
eISSN - 1477-9129
pISSN - 0950-1991
DOI - 10.1242/dev.164988
Subject(s) - biology , polarity (international relations) , caenorhabditis elegans , microbiology and biotechnology , embryo , actin , pi , genetics , gene , biochemistry , cell
Asymmetric division is crucial for embryonic development and stem cell lineages. In the one-cell C. elegans embryo, a contractile cortical actomyosin network contributes to asymmetric division by segregating PAR proteins to discrete cortical domains. Here, we discovered that the plasma membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) localizes to polarized dynamic structures in C. elegans zygotes, distributing in a PAR-dependent manner along the anterior-posterior (A-P) embryonic axis. PIP2 cortical structures overlap with F-actin, and coincide with the actin regulators RHO-1, CDC-42 as well as ECT-2. Particle image velocimetry analysis revealed that PIP2 and F-actin cortical movements are coupled, with PIP2 structures moving slightly ahead. Importantly, we established that PIP2 cortical structure formation and movement is actin-dependent. Conversely, we found that decreasing or increasing the level of PIP2 results in severe F-actin disorganization, revealing interdependence between these components. Furthermore, we uncovered that PIP2 and F-actin regulate the sizing of PAR cortical domains, including during the maintenance phase of polarization. Overall, our work establishes that a lipid membrane component, PIP2, modulates actin organization and cell polarity in C. elegans embryos.

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