Membrane Curvature and Lipid Composition Synergize To Regulate N-Ras Anchor Recruitment.

ABSTRACT: Proteins anchored to membranes through covalently linked fatty acids and/or isoprenoid groups play crucial roles in all forms of life. Sorting and trafficking of lipidated proteins has traditionally been discussed in the context of partitioning to membrane domains of different lipid composition. We recently showed that membrane shape/curvature can in itself mediate the recruitment of lipidated proteins. However, exactly how membrane curvature and composition synergize remains largely unexplored. Here we investigated how three critical structural parameters of lipids, namely acyl chain saturation, headgroup size, and acyl chain length, modulate the capacity of membrane curvature to recruit lipidated proteins. As a model system we used the lipidated minimal membrane anchor of the GTPase, N-R

SUBMITTER: Larsen JB 

PROVIDER: S-EPMC5607143 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature