Abstract：
:K-Ras is targeted to the plasma membrane by a C-terminal membrane anchor that comprises a farnesyl-cysteine-methyl-ester and a polybasic domain. We used quantitative spatial imaging and atomistic molecular dynamics simulations to examine molecular details of K-Ras plasma membrane binding. We found that the K-Ras anchor binds selected plasma membrane anionic lipids with defined head groups and lipid side chains. The precise amino acid sequence and prenyl group define a combinatorial code for lipid binding that extends beyond simple electrostatics; within this code lysine and arginine residues are non-equivalent and prenyl chain length modifies nascent polybasic domain lipid preferences. The code is realized by distinct dynamic tertiary structures of the anchor on the plasma membrane that govern amino acid side-chain-lipid interactions. An important consequence of this specificity is the ability of such anchors when aggregated to sort subsets of phospholipids into nanoclusters with defined lipid compositions that determine K-Ras signaling output.
journal_name
Celljournal_title
Cellauthors
Zhou Y,Prakash P,Liang H,Cho KJ,Gorfe AA,Hancock JFdoi
10.1016/j.cell.2016.11.059subject
Has Abstractpub_date
2017-01-12 00:00:00pages
239-251.e16issue
1-2eissn
0092-8674issn
1097-4172pii
S0092-8674(16)31674-9journal_volume
168pub_type
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