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Probing Colocalization of N‐Ras and K‐Ras4B Lipoproteins in Model Biomembranes
Author(s) -
Li Lei,
Dwivedi Mridula,
Patra Satyajit,
Erwin Nelli,
Möbitz Simone,
Winter Roland
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800776
Subject(s) - colocalization , membrane , chemistry , nanoclusters , förster resonance energy transfer , biophysics , membrane biology , biological membrane , vesicle , microbiology and biotechnology , fluorescence , biochemistry , biology , physics , organic chemistry , quantum mechanics
Signaling of N‐Ras and K‐Ras4B proteins depends strongly on their correct localization in the cell membrane. In vivo studies suggest that intermolecular interactions foster the self‐association of both N‐Ras and K‐Ras4B and the formation of nanoclusters in the cell membrane. As sites for effector binding, nanocluster formation is thought to be essential for effective signal transmission of both N‐Ras and K‐Ras4B. To shed more light on the spatial arrangement and mechanism underlying the proposed cross‐talk between spatially segregated Ras proteins, the simultaneous localization of N‐Ras and K‐Ras4B and their effect on the lateral organization of a heterogeneous model biomembrane has been studied by using AFM and FRET methodology. It is shown that, owing to the different natures of their membrane anchor systems, N‐Ras and K‐Ras4B not only avoid assembly in bulk solution and do not colocalize, but rather form individual nanoclusters that diffuse independently in the fluid membrane plane.