ArticleThe Journal of biological chemistry2012
Interaction surface and topology of Get3-Get4-Get5 protein complex, involved in targeting tail-anchored proteins to endoplasmic reticulum.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Characterisation of guided entry of tail-anchored proteins in Magnaporthe oryzae.PLoS pathogens · 2025Article
- Endoplasmic reticulum membrane receptors of the GET pathway are conserved throughout eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural and functional characterization of ybr137wp implicates its involvement in the targeting of tail-anchored proteins to membranes.Molecular and cellular biology · 2014Article
- Differential gradients of interaction affinities drive efficient targeting and recycling in the GET pathway.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Crystal structure of ATP-bound Get3-Get4-Get5 complex reveals regulation of Get3 by Get4.Nature structural & molecular biology · 2014Article
- Precise timing of ATPase activation drives targeting of tail-anchored proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The complex process of GETting tail-anchored membrane proteins to the ER.Current opinion in structural biology · 2012Review
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Authors and funding
6 authors.
Funding
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Abstract
Recent work has uncovered the "GET system," which is responsible for endoplasmic reticulum targeting of tail-anchored proteins. Although structural information and the individual roles of most components of this system have been defined, the interactions and interplay between them remain to be elucidated. Here, we investigated the interactions between Get3 and the Get4-Get5 complex from Saccharomyces cerevisiae. We show that Get3 interacts with Get4-Get5 via an interface dominated by electrostatic forces. Using isothermal titration calorimetry and small-angle x-ray scattering, we further demonstrate that the Get3 homodimer interacts with two copies of the Get4-Get5 complex to form an extended conformation in solution.
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