Transmembrane protein sorting driven by membrane curvature

H. Strahl, S. Ronneau, B. Solana González, D. Klutsch, C. Schaffner-Barbero, L. W. Hamoen

Résultats de recherche: Contribution à un journal/une revueArticle

Résumé

The intricate structure of prokaryotic and eukaryotic cells depends on the ability to target proteins to specific cellular locations. In most cases, we have a poor understanding of the underlying mechanisms. A typical example is the assembly of bacterial chemoreceptors at cell poles. Here we show that the classical chemoreceptor TlpA of Bacillus subtilis does not localize according to the consensus stochastic nucleation mechanism but accumulates at strongly curved membrane areas generated during cell division. This preference was confirmed by accumulation at non-septal curved membranes. Localization appears to be an intrinsic property of the protein complex and does not rely on chemoreceptor clustering, as was previously shown for Escherichia coli. By constructing specific amino-acid substitutions, we demonstrate that the preference for strongly curved membranes arises from the curved shape of chemoreceptor trimer of dimers. These findings demonstrate that the intrinsic shape of transmembrane proteins can determine their cellular localization.

langue originaleAnglais
Numéro d'article8728
journalNature Communications
Volume6
Les DOIs
étatPublié - 2 nov. 2015

Empreinte digitale

chemoreceptors
Protein Transport
classifying
Sorting
curvature
membranes
proteins
Membranes
Chemoreceptor Cells
Prokaryotic Cells
Proteins
Eukaryotic Cells
Bacilli
Amino Acid Substitution
Bacillus subtilis
cell division
Cell Division
Dimers
Escherichia coli
Cluster Analysis

Citer ceci

Strahl, H., Ronneau, S., González, B. S., Klutsch, D., Schaffner-Barbero, C., & Hamoen, L. W. (2015). Transmembrane protein sorting driven by membrane curvature. Nature Communications, 6, [8728]. https://doi.org/10.1038/ncomms9728
Strahl, H. ; Ronneau, S. ; González, B. Solana ; Klutsch, D. ; Schaffner-Barbero, C. ; Hamoen, L. W. / Transmembrane protein sorting driven by membrane curvature. Dans: Nature Communications. 2015 ; Vol 6.
@article{92da916f90054d5fa439f9c5d435f5a1,
title = "Transmembrane protein sorting driven by membrane curvature",
abstract = "The intricate structure of prokaryotic and eukaryotic cells depends on the ability to target proteins to specific cellular locations. In most cases, we have a poor understanding of the underlying mechanisms. A typical example is the assembly of bacterial chemoreceptors at cell poles. Here we show that the classical chemoreceptor TlpA of Bacillus subtilis does not localize according to the consensus stochastic nucleation mechanism but accumulates at strongly curved membrane areas generated during cell division. This preference was confirmed by accumulation at non-septal curved membranes. Localization appears to be an intrinsic property of the protein complex and does not rely on chemoreceptor clustering, as was previously shown for Escherichia coli. By constructing specific amino-acid substitutions, we demonstrate that the preference for strongly curved membranes arises from the curved shape of chemoreceptor trimer of dimers. These findings demonstrate that the intrinsic shape of transmembrane proteins can determine their cellular localization.",
author = "H. Strahl and S. Ronneau and Gonz{\'a}lez, {B. Solana} and D. Klutsch and C. Schaffner-Barbero and Hamoen, {L. W.}",
year = "2015",
month = "11",
day = "2",
doi = "10.1038/ncomms9728",
language = "English",
volume = "6",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

Strahl, H, Ronneau, S, González, BS, Klutsch, D, Schaffner-Barbero, C & Hamoen, LW 2015, 'Transmembrane protein sorting driven by membrane curvature', Nature Communications, VOL. 6, 8728. https://doi.org/10.1038/ncomms9728

Transmembrane protein sorting driven by membrane curvature. / Strahl, H.; Ronneau, S.; González, B. Solana; Klutsch, D.; Schaffner-Barbero, C.; Hamoen, L. W.

Dans: Nature Communications, Vol 6, 8728, 02.11.2015.

Résultats de recherche: Contribution à un journal/une revueArticle

TY - JOUR

T1 - Transmembrane protein sorting driven by membrane curvature

AU - Strahl, H.

AU - Ronneau, S.

AU - González, B. Solana

AU - Klutsch, D.

AU - Schaffner-Barbero, C.

AU - Hamoen, L. W.

PY - 2015/11/2

Y1 - 2015/11/2

N2 - The intricate structure of prokaryotic and eukaryotic cells depends on the ability to target proteins to specific cellular locations. In most cases, we have a poor understanding of the underlying mechanisms. A typical example is the assembly of bacterial chemoreceptors at cell poles. Here we show that the classical chemoreceptor TlpA of Bacillus subtilis does not localize according to the consensus stochastic nucleation mechanism but accumulates at strongly curved membrane areas generated during cell division. This preference was confirmed by accumulation at non-septal curved membranes. Localization appears to be an intrinsic property of the protein complex and does not rely on chemoreceptor clustering, as was previously shown for Escherichia coli. By constructing specific amino-acid substitutions, we demonstrate that the preference for strongly curved membranes arises from the curved shape of chemoreceptor trimer of dimers. These findings demonstrate that the intrinsic shape of transmembrane proteins can determine their cellular localization.

AB - The intricate structure of prokaryotic and eukaryotic cells depends on the ability to target proteins to specific cellular locations. In most cases, we have a poor understanding of the underlying mechanisms. A typical example is the assembly of bacterial chemoreceptors at cell poles. Here we show that the classical chemoreceptor TlpA of Bacillus subtilis does not localize according to the consensus stochastic nucleation mechanism but accumulates at strongly curved membrane areas generated during cell division. This preference was confirmed by accumulation at non-septal curved membranes. Localization appears to be an intrinsic property of the protein complex and does not rely on chemoreceptor clustering, as was previously shown for Escherichia coli. By constructing specific amino-acid substitutions, we demonstrate that the preference for strongly curved membranes arises from the curved shape of chemoreceptor trimer of dimers. These findings demonstrate that the intrinsic shape of transmembrane proteins can determine their cellular localization.

UR - http://www.scopus.com/inward/record.url?scp=84946208135&partnerID=8YFLogxK

U2 - 10.1038/ncomms9728

DO - 10.1038/ncomms9728

M3 - Article

AN - SCOPUS:84946208135

VL - 6

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 8728

ER -

Strahl H, Ronneau S, González BS, Klutsch D, Schaffner-Barbero C, Hamoen LW. Transmembrane protein sorting driven by membrane curvature. Nature Communications. 2015 nov. 2;6. 8728. https://doi.org/10.1038/ncomms9728