Catch-bond behaviour facilitates membrane tubulation by non-processive myosin 1b

Ayako Yamada, Alexandre Mamane, Jonathan Lee-Tin-Wah, Aurélie Di Cicco, Coline Prévost, Daniel Lévy, Jean-François Joanny, Evelyne Coudrier () and Patricia Bassereau ()
Additional contact information
Ayako Yamada: Institut Curie, Centre de Recherche
Alexandre Mamane: Institut Curie, Centre de Recherche
Jonathan Lee-Tin-Wah: Institut Curie, Centre de Recherche
Aurélie Di Cicco: Institut Curie, Centre de Recherche
Coline Prévost: Institut Curie, Centre de Recherche
Daniel Lévy: Institut Curie, Centre de Recherche
Jean-François Joanny: Institut Curie, Centre de Recherche
Evelyne Coudrier: Institut Curie, Centre de Recherche
Patricia Bassereau: Institut Curie, Centre de Recherche

Nature Communications, 2014, vol. 5, issue 1, 1-8

Abstract: Abstract 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.

Date: 2014
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms4624 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4624

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms4624

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().