Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting

One enigma in biology is the generation, sensing and maintenance of membrane curvature. Curvature-mediating proteins have been shown to induce specific membrane shapes by direct insertion and nanoscopic scaffolding, while the cytoskeletal motors exert forces indirectly through microtubule and actin...

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Autores principales: Rogez, Benoît, Würthner, Laeschkir, Petrova, Anastasiia B., Zierhut, Felix B., Saczko-Brack, Dario, Huergo, María Ana Cristina, Batters, Christopher, Frey, Erwin, Veigel, Claudia
Formato: Articulo
Lenguaje:Inglés
Publicado: 2019
Materias:
Química
Física
Ciencias Exactas
Myosin-VI
Membrane sculpting
Curvature-mediating proteins
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/123632
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-123632
record_format dspace
spelling I19-R120-10915-1236322024-02-22T18:34:29Z http://sedici.unlp.edu.ar/handle/10915/123632 Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting Rogez, Benoît Würthner, Laeschkir Petrova, Anastasiia B. Zierhut, Felix B. Saczko-Brack, Dario Huergo, María Ana Cristina Batters, Christopher Frey, Erwin Veigel, Claudia 2019-07-24 2021-08-27T15:08:38Z en Química Física Ciencias Exactas Myosin-VI Membrane sculpting Curvature-mediating proteins One enigma in biology is the generation, sensing and maintenance of membrane curvature. Curvature-mediating proteins have been shown to induce specific membrane shapes by direct insertion and nanoscopic scaffolding, while the cytoskeletal motors exert forces indirectly through microtubule and actin networks. It remains unclear, whether the manifold direct motorprotein–lipid interactions themselves constitute another fundamental route to remodel the membrane shape. Here we show, combining super-resolution-fluorescence microscopy and membrane-reshaping nanoparticles, that curvature-dependent lipid interactions of myosin-VI on its own, remarkably remodel the membrane geometry into dynamic spatial patterns on the nano- to micrometer scale. We propose a quantitative theoretical model that explains this dynamic membrane sculpting mechanism. The emerging route of motorprotein–lipid interactions reshaping membrane morphology by a mechanism of feedback and instability opens up hitherto unexplored avenues of membrane remodelling and links cytoskeletal motors to early events in the sequence of membrane sculpting in eukaryotic cell biology. Curvature-mediating proteins are known to induce specific membrane shapes, but whether motorprotein-lipid interactions remodel membranes too remains unclear. Here authors show that curvature-dependent lipid interactions of myosin-VI remodel the membrane geometry into dynamic spatial patterns. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas Articulo Articulo http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) application/pdf
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Física
Ciencias Exactas
Myosin-VI
Membrane sculpting
Curvature-mediating proteins
spellingShingle Química
Física
Ciencias Exactas
Myosin-VI
Membrane sculpting
Curvature-mediating proteins
Rogez, Benoît
Würthner, Laeschkir
Petrova, Anastasiia B.
Zierhut, Felix B.
Saczko-Brack, Dario
Huergo, María Ana Cristina
Batters, Christopher
Frey, Erwin
Veigel, Claudia
Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting
topic_facet Química
Física
Ciencias Exactas
Myosin-VI
Membrane sculpting
Curvature-mediating proteins
description One enigma in biology is the generation, sensing and maintenance of membrane curvature. Curvature-mediating proteins have been shown to induce specific membrane shapes by direct insertion and nanoscopic scaffolding, while the cytoskeletal motors exert forces indirectly through microtubule and actin networks. It remains unclear, whether the manifold direct motorprotein–lipid interactions themselves constitute another fundamental route to remodel the membrane shape. Here we show, combining super-resolution-fluorescence microscopy and membrane-reshaping nanoparticles, that curvature-dependent lipid interactions of myosin-VI on its own, remarkably remodel the membrane geometry into dynamic spatial patterns on the nano- to micrometer scale. We propose a quantitative theoretical model that explains this dynamic membrane sculpting mechanism. The emerging route of motorprotein–lipid interactions reshaping membrane morphology by a mechanism of feedback and instability opens up hitherto unexplored avenues of membrane remodelling and links cytoskeletal motors to early events in the sequence of membrane sculpting in eukaryotic cell biology. Curvature-mediating proteins are known to induce specific membrane shapes, but whether motorprotein-lipid interactions remodel membranes too remains unclear. Here authors show that curvature-dependent lipid interactions of myosin-VI remodel the membrane geometry into dynamic spatial patterns.
format Articulo
Articulo
author Rogez, Benoît
Würthner, Laeschkir
Petrova, Anastasiia B.
Zierhut, Felix B.
Saczko-Brack, Dario
Huergo, María Ana Cristina
Batters, Christopher
Frey, Erwin
Veigel, Claudia
author_facet Rogez, Benoît
Würthner, Laeschkir
Petrova, Anastasiia B.
Zierhut, Felix B.
Saczko-Brack, Dario
Huergo, María Ana Cristina
Batters, Christopher
Frey, Erwin
Veigel, Claudia
author_sort Rogez, Benoît
title Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting
title_short Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting
title_full Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting
title_fullStr Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting
title_full_unstemmed Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting
title_sort reconstitution reveals how myosin-vi self-organises to generate a dynamic mechanism of membrane sculpting
publishDate 2019
url http://sedici.unlp.edu.ar/handle/10915/123632
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