Catch-bond behaviour facilitates membrane tubulation by non-processive myosin 1b.
Myosin 1b is a single-headed membrane-associated motor that binds to actin filaments with a catch-bond behaviour in response to load. In vivo, myosin 1b is required to form membrane tubules at both endosomes and the trans-Golgi network. To establish the link between these two fundamental properties, here we investigate the capacity of myosin 1b to extract membrane tubes along bundled actin filaments in a minimal reconstituted system. We show that single-headed non-processive myosin 1b can extract membrane tubes at a biologically relevant low density. In contrast to kinesins we do not observe motor accumulation at the tip, suggesting that the underlying mechanism for tube formation is different. In our theoretical model, myosin 1b catch-bond properties facilitate tube extraction under conditions of increasing membrane tension by reducing the density of myo1b required to pull tubes.
1] Institut Curie, Centre de Recherche, Paris F-75248, France [2] CNRS, UMR 168, PhysicoChimie Curie, Paris F-75248, France [3] CNRS, UMR144, Compartimentation et dynamique cellulaires, Paris F-75248, France [4] Université Pierre et Marie Curie, Paris F-75252, France [5] Labex CelTisPhyBio and Paris Sciences et Lettres, Paris F-75005, France [6].
Ayako
A
Yamada
1] Institut Curie, Centre de Recherche, Paris F-75248, France [2] CNRS, UMR 168, PhysicoChimie Curie, Paris F-75248, France [3] Université Pierre et Marie Curie, Paris F-75252, France [4] Labex CelTisPhyBio and Paris Sciences et Lettres, Paris F-75005, France [5].
Alexandre
A
Mamane
1] Institut Curie, Centre de Recherche, Paris F-75248, France [2] CNRS, UMR 168, PhysicoChimie Curie, Paris F-75248, France [3] Université Pierre et Marie Curie, Paris F-75252, France [4] Labex CelTisPhyBio and Paris Sciences et Lettres, Paris F-75005, France.
Jonathan
J
Lee-Tin-Wah
1] Institut Curie, Centre de Recherche, Paris F-75248, France [2] CNRS, UMR 168, PhysicoChimie Curie, Paris F-75248, France [3] Université Pierre et Marie Curie, Paris F-75252, France [4] Labex CelTisPhyBio and Paris Sciences et Lettres, Paris F-75005, France.
Aurélie
A
Di Cicco
1] Institut Curie, Centre de Recherche, Paris F-75248, France [2] CNRS, UMR 168, PhysicoChimie Curie, Paris F-75248, France [3] Université Pierre et Marie Curie, Paris F-75252, France [4] Labex CelTisPhyBio and Paris Sciences et Lettres, Paris F-75005, France.
Coline
C
Prévost
1] Institut Curie, Centre de Recherche, Paris F-75248, France [2] CNRS, UMR 168, PhysicoChimie Curie, Paris F-75248, France [3] Université Pierre et Marie Curie, Paris F-75252, France [4] Labex CelTisPhyBio and Paris Sciences et Lettres, Paris F-75005, France [5] Cell and Tissue Imaging Facility (PICT-IBiSA), Institut Curie, Paris F-75248, France.
Daniel
D
Lévy
1] Institut Curie, Centre de Recherche, Paris F-75248, France [2] CNRS, UMR 168, PhysicoChimie Curie, Paris F-75248, France [3] Université Pierre et Marie Curie, Paris F-75252, France [4] Labex CelTisPhyBio and Paris Sciences et Lettres, Paris F-75005, France.
Jean-François
JF
Joanny
1] Institut Curie, Centre de Recherche, Paris F-75248, France [2] CNRS, UMR144, Compartimentation et dynamique cellulaires, Paris F-75248, France [3] Labex CelTisPhyBio and Paris Sciences et Lettres, Paris F-75005, France [4].
Evelyne
E
Coudrier
1] Institut Curie, Centre de Recherche, Paris F-75248, France [2] CNRS, UMR 168, PhysicoChimie Curie, Paris F-75248, France [3] Université Pierre et Marie Curie, Paris F-75252, France [4] Labex CelTisPhyBio and Paris Sciences et Lettres, Paris F-75005, France [5].
Patricia
P
Bassereau
D008841:Actin Cytoskeleton / Q000378:metabolism*; D011992:Endosomes / Q000378:metabolism; D006801:Humans; D016547:Kinesins / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism*; D024461:Myosin Type I / Q000378:metabolism*; D021601:trans-Golgi Network / Q000378:metabolism*
C000594736:MYO1B protein, human; D024461:Myosin Type I; D016547:Kinesins