Format:
Online-Ressource
ISSN:
1439-7641
Content:
Abstract: Plasma‐membrane‐associated Ras proteins typically control signal transduction processes. As nanoclustering and membrane viscosity sensing provide plausible signaling mechanisms, determination of the rotational and translational dynamics of membrane‐bound Ras isoforms can help to link their dynamic mobility to their function. Herein, by using time‐resolved fluorescence anisotropy and correlation spectroscopic measurements, we obtain the rotational‐correlation time and the translational diffusion coefficient of lipidated boron‐dipyrromethene‐labeled Ras, both in bulk Ras and upon membrane binding. The results show that the second lipidation motif of N‐Ras triggers dimer formation in bulk solution, whereas K‐Ras4B is monomeric. Upon membrane binding, an essentially free rotation of the G‐domain is observed, along with a high lateral mobility; the latter is essentially limited by the viscosity of the membrane and by lipid‐mediated electrostatic interactions. This high diffusional mobility warrants rapid recognition–binding sequences in the membrane‐bound state, thereby facilitating efficient interactions between the Ras proteins and scaffolding or effector proteins. The lipid‐like rapid lateral diffusion observed here complies with in vivo data.
In:
volume:14
In:
number:16
In:
year:2013
In:
pages:3698-3705
In:
extent:8
In:
ChemPhysChem, Weinheim : Wiley-VCH Verl., [2000]-, 14, Heft 16 (2013), 3698-3705 (gesamt 8), 1439-7641
Language:
English
DOI:
10.1002/cphc.201300617
URN:
urn:nbn:de:101:1-2023020405241390008232
URL:
https://doi.org/10.1002/cphc.201300617
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2023020405241390008232
URL:
https://d-nb.info/1280042648/34
URL:
https://doi.org/10.1002/cphc.201300617