Functional recruitment of dynamin requires multimeric interactions for efficient endocytosis

Morgane Rosendale, Thi Nhu Ngoc Van, Dolors Grillo-Bosch, Silvia Sposini, Léa Claverie, Isabel Gauthereau, Stéphane Claverol, Daniel Choquet, Matthieu Sainlos () and David Perrais ()
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Morgane Rosendale: University of Bordeaux
Thi Nhu Ngoc Van: University of Bordeaux
Dolors Grillo-Bosch: University of Bordeaux
Silvia Sposini: University of Bordeaux
Léa Claverie: University of Bordeaux
Isabel Gauthereau: University of Bordeaux
Stéphane Claverol: University of Bordeaux
Daniel Choquet: University of Bordeaux
Matthieu Sainlos: University of Bordeaux
David Perrais: University of Bordeaux

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract During clathrin mediated endocytosis (CME), the concerted action of dynamin and its interacting partners drives membrane scission. Essential interactions occur between the proline/arginine-rich domain of dynamin (dynPRD) and the Src-homology domain 3 (SH3) of various proteins including amphiphysins. Here we show that multiple SH3 domains must bind simultaneously to dynPRD through three adjacent motifs for dynamin’s efficient recruitment and function. First, we show that mutant dynamins modified in a single motif, including the central amphiphysin SH3 (amphSH3) binding motif, partially rescue CME in dynamin triple knock-out cells. However, mutating two motifs largely prevents that ability. Furthermore, we designed divalent dynPRD-derived peptides. These ligands bind multimers of amphSH3 with >100-fold higher affinity than monovalent ones in vitro. Accordingly, dialyzing living cells with these divalent peptides through a patch-clamp pipette blocks CME much more effectively than with monovalent ones. We conclude that dynamin drives vesicle scission via multivalent interactions in cells.

Date: 2019
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DOI: 10.1038/s41467-019-12434-9

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