Differential gradients of interaction affinities drive efficient targeting and recycling in the GET pathway.

ABSTRACT: Efficient and accurate localization of membrane proteins requires a complex cascade of interactions between protein machineries. This requirement is exemplified in the guided entry of tail-anchored (TA) protein (GET) pathway, where the central targeting factor Get3 must sequentially interact with three distinct binding partners to ensure the delivery of TA proteins to the endoplasmic reticulum (ER) membrane. To understand the molecular principles that provide the vectorial driving force of these interactions, we developed quantitative fluorescence assays to monitor Get3-effector interactions at each stage of targeting. We show that nucleotide and substrate generate differential gradients of interaction energies that drive the ordered interaction of Get3 with successive effectors. These dat

SUBMITTER: Rome ME 

PROVIDER: S-EPMC4246279 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature