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The structural basis for regulation of the glutathione transporter Ycf1 by regulatory domain phosphorylation
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The structural basis for regulation of the glutathione transporter Ycf1 by regulatory domain phosphorylation
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Journal Article
The structural basis for regulation of the glutathione transporter Ycf1 by regulatory domain phosphorylation
2022
Overview
Yeast Cadmium Factor 1 (Ycf1) sequesters heavy metals and glutathione into the vacuole to counter cell stress. Ycf1 belongs to the ATP binding cassette C-subfamily (ABCC) of transporters, many of which are regulated by phosphorylation on intrinsically-disordered domains. The regulatory mechanism of phosphorylation is still poorly understood. Here, we report two cryo-EM structures of Ycf1 at 3.4 Å and 4.0 Å resolution in inward-facing open conformations that capture previously unobserved ordered states of the intrinsically disordered regulatory domain (R-domain). R-domain phosphorylation is clearly evident and induces a topology promoting electrostatic and hydrophobic interactions with Nucleotide Binding Domain 1 (NBD1) and the Lasso motif. These interactions stay constant between the structures and are related by rigid body movements of the NBD1/R-domain complex. Biochemical data further show R-domain phosphorylation reorganizes the Ycf1 architecture and is required for maximal ATPase activity. Together, we provide insights into how R-domains control ABCC transporter activity.
Ycf1, a C-family member ATP Binding Cassette (ABC) transporter, transports glutathione and glutathione-metal complexes in yeast. Here the authors use cryo-EM and biochemical analysis to show how an intrinsically-disordered regulatory domain (R-domain) controls activity upon phosphorylation by engaging with a Nucleotide Binding Domain.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 101/58
/ 82/80
/ 82/83
/ ATP-Binding Cassette Transporters - metabolism
/ Binding
/ Cadmium
/ Domains
/ Humanities and Social Sciences
/ INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
/ Kinases
/ Regulatory mechanisms (biology)
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - metabolism
/ Science
/ Topology
/ Yeast
