ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- The Power of Protein Dynamics in Binding and Allostery.Biochemistry · 2026Review
- Remote on-off switching of protein activity by intrinsically disordered region.Nature structural & molecular biology · 2025Article
- Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad.Nature communications · 2024Article
- Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond.International journal of molecular sciences · 2023Review
- A conserved guided entry of tail-anchored pathway is involved in the trafficking of a subset of membrane proteins in Plasmodium falciparum.PLoS pathogens · 2021Article
- Capture and delivery of tail-anchored proteins to the endoplasmic reticulum.The Journal of cell biology · 2021Review
- The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove.Protein science : a publication of the Protein Society · 2021Article
- Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade.The Journal of biological chemistry · 2019Review
- TPR-containing proteins control protein organization and homeostasis for the endoplasmic reticulum.Critical reviews in biochemistry and molecular biology · 2019Review
- The roles of cytosolic quality control proteins, SGTA and the BAG6 complex, in disease.Advances in protein chemistry and structural biology · 2019Review
- Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.BMC biology · 2018Article
- Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion.Annual review of cell and developmental biology · 2017Review
- Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.Frontiers in molecular biosciences · 2017Article
- SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism.Scientific reports · 2016Article
- Ubiquitin-like domains can target to the proteasome but proteolysis requires a disordered region.The EMBO journal · 2016Article
- Structural and functional insights into the E3 ligase, RNF126.Scientific reports · 2016Article
- Extension of a protein docking algorithm to membranes and applications to amyloid precursor protein dimerization.Proteins · 2015Article
- Structural and Functional Insights into Small, Glutamine-Rich, Tetratricopeptide Repeat Protein Alpha.Frontiers in molecular biosciences · 2015Review
- SGTA regulates the cytosolic quality control of hydrophobic substrates.Journal of cell science · 2014Article
- Article
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7 authors.
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Abstract
Small, glutamine-rich, tetratricopeptide repeat protein 2 (Sgt2) is the first known port of call for many newly synthesized tail-anchored (TA) proteins released from the ribosome and destined for the GET (Guided Entry of TA proteins) pathway. This leads them to the residential membrane of the endoplasmic reticulum via an alternative to the cotranslational, signal recognition particle-dependent mechanism that their topology denies them. In yeast, the first stage of the GET pathway involves Sgt2 passing TA proteins on to the Get4/Get5 complex through a direct interaction between the N-terminal (NT) domain of Sgt2 and the ubiquitin-like (UBL) domain of Get5. Here we characterize this interaction at a molecular level by solving both a solution structure of Sgt2_NT, which adopts a unique helical fold, and a crystal structure of the Get5_UBL. Furthermore, using reciprocal chemical shift perturbation data and experimental restraints, we solve a structure of the Sgt2_NT/Get5_UBL complex, validate it via site-directed mutagenesis, and empirically determine its stoichiometry using relaxation experiments and isothermal titration calorimetry. Taken together, these data provide detailed structural information about the interaction between two key players in the coordinated delivery of TA protein substrates into the GET pathway.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.