Jump to main content
Jump to site search

Issue 47, 2012
Previous Article Next Article

Shape as a determinant of membrane protein cluster formation

Author affiliations

Abstract

Cluster formation of membrane proteins is a crucial event in many vital cellular processes. Here, we present a thorough examination of the oligomerisation ability of membrane proteins with different geometries. By means of mesoscopic membrane simulations we show that lipid-mediated interactions between proteins depend both on the shape of the hydrophobic domain of the proteins and on their hydrophobic mismatch. Based on that, we find that protein interactions can be either attractive or repulsive, depending on the characteristic bilayer perturbations induced by the proteins. The influence of these perturbations is quantified via the associated potential of mean force. Such geometry-dependent interactions are likely to fine-tune protein oligomerization events during cellular processes, for example signal transduction or protein sorting.

Graphical abstract: Shape as a determinant of membrane protein cluster formation

Back to tab navigation

Article information


Submitted
25 Jul 2012
Accepted
14 Sep 2012
First published
04 Oct 2012

Soft Matter, 2012,8, 11905-11910
Article type
Paper

Shape as a determinant of membrane protein cluster formation

D. Morozova, M. Weiss and G. Guigas, Soft Matter, 2012, 8, 11905 DOI: 10.1039/C2SM26720A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.


Social activity

Search articles by author

Spotlight

Advertisements