ArticleBiology direct2017
Recognition of a structural domain (RWDBD) in Gcn1 proteins that interacts with the RWD domain containing proteins.
Article in Biology direct, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- A genetic approach to identify amino acids in human GCN1 required for mediating Gcn2 activation.microPublication biology · 2026Article
- Highly expressed GCN1 is associated with cancer progression and poor prognosis in hepatocellular carcinoma patients.Cancer cell international · 2025Article
- The protein kinases family in fungi: adaptability, virulence and conservation between species.Frontiers in microbiology · 2025Review
- Evidence that Xrn1 is in complex with Gcn1, and is required for full levels of eIF2α phosphorylation.The Biochemical journal · 2024Article
- Emerging Role of GCN1 in Disease and Homeostasis.International journal of molecular sciences · 2024Review
- RNAi-Mediated Knockdown of Acidic Ribosomal Stalk Protein P1 Arrests Egg Development in Adult Female Yellow Fever Mosquitoes,Insects · 2024Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protein Gcn1 (General control non-derepressible 1) is found in virtually all eukaryotes, and is a key component of the general amino acid control signal transduction pathway. This pathway is best known for its importance for cells to sense and overcome amino acid starvation. Gcn1 directly binds to the RWD (RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases) domain of the protein kinase Gcn2, and this is essential for delivering the starvation signal to Gcn2. Gcn2, and thus the GAAC (General Amino Acid Control) pathway, then becomes activated enabling the cell to cope and overcome the starvation condition. Using sensitive homology detection and fold recognition methods a conserved structural domain in Gcn1, RWD Binding Domain (RWDBD), has been recognized that encompasses the region experimentally shown previously to be involved in Gcn2 binding. Further, the structural fold for this domain has been recognized as the ARM (Armadillo) domain, and residues likely to be involved in the binding of Gcn2 RWD domain have been identified within this structural domain. Thus, the current analysis provides a structural basis of Gcn1-Gcn2 association. REVIEWERS: This article was reviewed by Dr Oliviero Carugo and Dr Michael Gromiha.
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