Endothelial cell rearrangements during vascular patterning require PI3-kinase-mediated inhibition of actomyosin contractility View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-11-16

AUTHORS

Ana Angulo-Urarte, Pedro Casado, Sandra D. Castillo, Piotr Kobialka, Maria Paraskevi Kotini, Ana M. Figueiredo, Pau Castel, Vinothini Rajeeve, Maria Milà-Guasch, Jaime Millan, Cora Wiesner, Helena Serra, Laia Muixi, Oriol Casanovas, Francesc Viñals, Markus Affolter, Holger Gerhardt, Stephan Huveneers, Heinz-Georg Belting, Pedro R. Cutillas, Mariona Graupera

ABSTRACT

Angiogenesis is a dynamic process relying on endothelial cell rearrangements within vascular tubes, yet the underlying mechanisms and functional relevance are poorly understood. Here we show that PI3Kα regulates endothelial cell rearrangements using a combination of a PI3Kα-selective inhibitor and endothelial-specific genetic deletion to abrogate PI3Kα activity during vessel development. Quantitative phosphoproteomics together with detailed cell biology analyses in vivo and in vitro reveal that PI3K signalling prevents NUAK1-dependent phosphorylation of the myosin phosphatase targeting-1 (MYPT1) protein, thereby allowing myosin light chain phosphatase (MLCP) activity and ultimately downregulating actomyosin contractility. Decreased PI3K activity enhances actomyosin contractility and impairs junctional remodelling and stabilization. This leads to overstretched endothelial cells that fail to anastomose properly and form aberrant superimposed layers within the vasculature. Our findings define the PI3K/NUAK1/MYPT1/MLCP axis as a critical pathway to regulate actomyosin contractility in endothelial cells, supporting vascular patterning and expansion through the control of cell rearrangement. More... »

PAGES

4826

References to SciGraph publications

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  • Journal

    TITLE

    Nature Communications

    ISSUE

    1

    VOLUME

    9

    Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41467-018-07172-3

    DOI

    http://dx.doi.org/10.1038/s41467-018-07172-3

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1109859639

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/30446640


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