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A cross-talk between PI(4,5)P2 and CK2 modulates actin remodeling during endocytic uptake

AutorFernández-Golbano, Isabel María; Idrissi, Fátima-Zahra ; Giblin, Jonathan; Grosshans, Bianka L.; Robles, Virginia; Grötsch, Helga; Borrás, María del Mar; Geli, María Isabel
Fecha de publicación15-jun-2014
CitaciónGordon Conference on Lysosomes & Endocytosis (2014)
ResumenA transient burst of actin polymerization assists endocytic budding. How actin polymerization is controlled in this context is not understood. Here, we show that a crosstalk between PI(4,5)P2 and the CK2 catalytic subunit Cka2, controls actin polymerization at endocytic sites. We find that phosphorylation of the myosin-I Myo5 by Cka2 down-regulates Myo5-induced Arp2/3-dependent actin polymerization whereas PI(4,5)P2 cooperatively relieves Myo5 autoinhibition and inhibits the catalytic activity of Cka2. Cka2 and the PI(4,5)P2 5-phosphatases Sjl1 and Sjl2, the yeast synaptojanins, exhibit genetic interactions indicating functional redundancy. The ultrastructural analysis of plasma membrane invaginations in CK2 and Synaptojanin mutants demonstrate that both cooperate to initiate constriction of the invagination neck, a process coupled to the remodeling of the endocytic actin network. Our data demonstrate a novel holoenzyme-independent function of CK2 in endocytic budding and establish a robust genetic, functional and molecular link between PI(4,5)P2 and CK2, two masters of intracellular signaling.
DescripciónTrabajo presentado en la Gordon Conference on Lysosomes & Endocytosis, celebrada en Andover, New Hampshire, Estados Unidos, del 15 all 20 de junio de 2014
URIhttp://hdl.handle.net/10261/158361
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