Shape matters in protein mobility within membranes.
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.
Institut Curie, Centre de Recherche, F-75248 Paris, France.
François
F
Quemeneur
Jon K
JK
Sigurdsson
Marianne
M
Renner
Paul J
PJ
Atzberger
Patricia
P
Bassereau
David
D
Lacoste
D020346:Aquaporins / Q000378:metabolism; D048430:Cell Shape; D005136:Eye Proteins / Q000378:metabolism; D008051:Lipid Bilayers; D008565:Membrane Proteins / Q000378:metabolism*; D024642:Potassium Channels, Voltage-Gated / Q000378:metabolism; D021381:Protein Transport
D020346:Aquaporins; D005136:Eye Proteins; D008051:Lipid Bilayers; D008565:Membrane Proteins; D024642:Potassium Channels, Voltage-Gated; C030328:aquaporin 0
Brownian motion; Saffman–Delbrück; drag force; internal membrane structure; micropipette aspiration