K-Ras4B Remains Monomeric on Membranes over a Wide Range of Surface Densities and Lipid Compositions.

Abstract:

:Ras is a membrane-anchored signaling protein that serves as a hub for many signaling pathways and also plays a prominent role in cancer. The intrinsic behavior of Ras on the membrane has captivated the biophysics community in recent years, especially the possibility that it may form dimers. In this article, we describe results from a comprehensive series of experiments using fluorescence correlation spectroscopy and single-molecule tracking to probe the possible dimerization of natively expressed and fully processed K-Ras4B in supported lipid bilayer membranes. Key to these studies is the fact that K-Ras4B has its native membrane anchor, including both the farnesylation and methylation of the terminal cysteine, enabling detailed exploration of possible effects of cholesterol and lipid composition on K-Ras4B membrane organization. The results from all conditions studied indicate that full-length K-Ras4B lacks intrinsic dimerization capability. This suggests that any lateral organization of Ras in living cell membranes likely stems from interactions with other factors.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Chung JK,Lee YK,Denson JP,Gillette WK,Alvarez S,Stephen AG,Groves JT

doi

10.1016/j.bpj.2017.10.042

subject

Has Abstract

pub_date

2018-01-09 00:00:00

pages

137-145

issue

1

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(17)31205-5

journal_volume

114

pub_type

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