| Title: |
Membrane Shape Modulates Transmembrane Protein Distribution |
| Authors: |
Aimon, Sophie; Callan-Jones, Andrew; Berthaud, Alice; Pinot, Mathieu; Toombes, Gilman E S; Bassereau, Patricia |
| Contributors: |
Physico-Chimie-Curie (PCC); Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie Paris -Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS); Kavli Institute for Brain and Mind San Diego; University of California San Diego (UC San Diego); University of California (UC)-University of California (UC); Matière et Systèmes Complexes (MSC); Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS); Université Paris Sciences et Lettres (PSL); Biologie Cellulaire et Cancer; Institut Curie Paris -Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS); National Institute of Neurological Disorders and Stroke Bethesda (NINDS); National Institutes of Health Bethesda, MD, USA (NIH); The authors acknowledge financial support from the Agence Nationale de la Recherche (grant BLAN-0057-01), the Fédération “Dynamique des systèmes complexes hors équilibre” of the University Pierre et Marie Curie, the Institut Curie, and the “Fondation pour la Recherche Médicale” (to S.A.), CNRS action “Prise de Risque” (to A.B.), a Marie Curie fellowship (to G.E.S.T.), and the French research consortium “CellTiss” (to P.B.). |
| Source: |
ISSN: 1534-5807. |
| Publisher Information: |
CCSD; Elsevier |
| Publication Year: |
2014 |
| Subject Terms: |
[SDV]Life Sciences [q-bio]; [PHYS.COND.CM-SCM]Physics [physics]/Condensed Matter [cond-mat]/Soft Condensed Matter [cond-mat.soft]; [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry; Molecular Biology/Biophysics; [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] |
| Description: |
International audience ; Although membrane shape varies greatly throughout the cell, the contribution of membrane curvature to transmembrane protein targeting is unknown because of the numerous sorting mechanisms that take place concurrently in cells. To isolate the effect of membrane shape, we used cell-sized giant unilamellar vesicles (GUVs) containing either the potassium channel KvAP or the water channel AQP0 to form membrane nanotubes with controlled radii. Whereas the AQP0 concentrations in flat and curved membranes were indistinguishable, KvAP was enriched in the tubes, with greater enrichment in more highly curved membranes. Fluorescence recovery after photobleaching measurements showed that both proteins could freely diffuse through the neck between the tube and GUV, and the effect of each protein on membrane shape and stiffness was characterized using a thermodynamic sorting model. This study establishes the importance of membrane shape for targeting transmembrane proteins and provides a method for determining the effective shape and flexibility of membrane proteins. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| Relation: |
info:eu-repo/semantics/altIdentifier/pmid/24480645; PUBMED: 24480645; PUBMEDCENTRAL: PMC3954780 |
| DOI: |
10.1016/j.devcel.2013.12.012 |
| Availability: |
https://hal.science/hal-05371495; https://hal.science/hal-05371495v1/document; https://hal.science/hal-05371495v1/file/nihms557548.pdf; https://doi.org/10.1016/j.devcel.2013.12.012 |
| Rights: |
http://hal.archives-ouvertes.fr/licences/copyright/ ; info:eu-repo/semantics/OpenAccess |
| Accession Number: |
edsbas.B8FE20B5 |
| Database: |
BASE |