期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 111, 期 14, 页码 5083-5087出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1321054111
关键词
Brownian motion; Saffman-Delbruck; internal membrane structure; drag force; micropipette aspiration
资金
- Agence Nationale pour la Recherche
- Fondation Pierre-Gilles de Gennes
- France Parkinson
- Department of Energy [CM4]
- National Science Foundation-CAREER [DMS-0956210]
- Chinese Academy of Sciences [KJCX2.YW.W10]
- Direct For Mathematical & Physical Scien
- Division Of Mathematical Sciences [0956210] Funding Source: National Science Foundation
The lateral mobility of proteins within cell membranes is usually thought to be dependent on their size and modulated by local heterogeneities of the membrane. Experiments using single-particle tracking on reconstituted membranes demonstrate that protein diffusion is significantly influenced by the interplay of membrane curvature, membrane tension, and protein shape. We find that the curvature-coupled voltage-gated potassium channel (KvAP) undergoes a significant increase in protein mobility under tension, whereas the mobility of the curvature-neutral water channel aquaporin 0 (AQP0) is insensitive to it. Such observations are well explained in terms of an effective friction coefficient of the protein induced by the local membrane deformation.
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