F-BAR domain protein Syndapin regulates actomyosin dynamics during apical cap remodeling in syncytial Drosophila embryos

Aparna Sherlekar (1) , Gayatri Mundhe (1, 2) , Prachi Richa (1) , Bipasha Dey (1) , Swati Sharma (1) , Richa Rikhy (1)

1 IISER Pune - Indian Institute of Science Education and Research Pune
2 IBDM - Institut de Biologie du Développement de Marseille

Branched actin networks driven by Arp2/3 interact with actomyosin filaments in processes such as cell migration. Similar interactions occur in the syncytial Drosophila blastoderm embryo where expansion of apical caps by Arp2/3-driven actin polymerization occurs in interphase, and cap buckling at contact edges by Myosin II to form furrows takes place in metaphase. Here, we study the role of Syndapin (Synd), an F-BAR domain-containing protein, in apical cap remodeling prior to furrow extension. We found that depletion of synd resulted in larger apical caps. Super-resolution and TIRF microscopy showed that control embryos had long apical actin protrusions in caps during interphase and short protrusions during metaphase, whereas synd depletion led to formation of sustained long protrusions, even during metaphase. Loss of Arp2/3 function in synd mutants partly reverted defects in apical cap expansion and protrusion remodeling. Myosin II levels were decreased in synd mutants, an observation consistent with the expanded cap phenotype previously reported for Myosin II mutant embryos. We propose that Synd function limits branching activity during cap expansion and affects Myosin II distribution in order to bring about a transition in actin remodeling activity from apical cap expansion to lateral furrow extension.

Mots clés: Actomyosin; Syndapin; Cap; Metaphase furrow; Drosophila

Domaines: Sciences du Vivant [q-bio]

Aparna Sherlekar, Gayatri Mundhe, Prachi Richa, Bipasha Dey, Swati Sharma, et al.. F-BAR domain protein Syndapin regulates actomyosin dynamics during apical cap remodeling in syncytial Drosophila embryos. Journal of Cell Science, 2020, 133, ⟨10.1242/jcs.235846⟩. ⟨hal-03141809⟩