ArticlePloS one2010
Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 136 citations in OpenAlex.
- Swine GBP1 restricts PDCoV replication via disrupting the replication and transcription complex formation.Journal of virology · 2026Article
- Article
- VSIG2 as a novel immunosuppressive ligand interacts with Nectin-2 to regulate T cell responses.Journal of neuroinflammation · 2025Article
- Guanylate-binding proteins: emerging critical functions in plant development, immunity and stress response.The New phytologist · 2025Review
- Molecular mechanisms and functions of guanylate-binding protein 2 in inflammation and cancer (Review).Oncology letters · 2025Review
- Deciphering the origins of guanylate-binding proteins in mammals (Monotreme, Marsupials and Placentals).BMC biology · 2025Article
- Guanylate-binding protein 5: a promising biomarker and therapeutic target.Infection and immunity · 2025Review
- Guanylate binding proteins (GBPs) as novel therapeutic targets against single-stranded RNA viruses.Molecular biology reports · 2025Review
- Bat-specific adaptations in interferon signaling and GBP1 contribute to enhanced antiviral capacity.Nature communications · 2025Article
- Multifaceted Roles of Guanylate-Binding Proteins in Cancer.International journal of molecular sciences · 2025Review
- Structural basis of antimicrobial membrane coat assembly by human GBP1.Nature structural & molecular biology · 2025Article
- From mechanisms to therapies: the multifaceted roles of guanylate-binding protein 2 in immunity, cancer, and beyond.Frontiers in immunology · 2025Review
- The Large GTPase Guanylate-Binding Protein-1 (GBP-1) Promotes Mitochondrial Fission in Glioblastoma.International journal of molecular sciences · 2024Article
- Mouse guanylate-binding proteins of the chromosome 3 cluster do not mediate antiviral activity in vitro or in mouse models of infection.Communications biology · 2024Article
- Immune checkpoint gene signature assesses immune infiltration profiles in bladder cancer and identifies KRT23 as an immunotherapeutic target.BMC cancer · 2024Article
- Guanylate-binding protein 1 acts as a pro-viral factor for the life cycle of hepatitis C virus.PLoS pathogens · 2024Article
- Structural insights into the activation mechanism of antimicrobial GBP1.The EMBO journal · 2024Article
- Evolutionary and functional characterization of lagomorph guanylate-binding proteins: a story of gain and loss and shedding light on expression, localization and innate immunity-related functions.Frontiers in immunology · 2024Article
- Guanylate-binding protein-5 is involved in inflammasome activation by bacterial DNA but only the cooperation of multiple GBPs accounts for control ofFrontiers in immunology · 2024Article
- Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Guanylate-binding proteins (GBPs) belong to the dynamin family of large GTPases and represent the major IFN-γ-induced proteins. Here we systematically investigated the mechanisms regulating the subcellular localization of GBPs. Three GBPs (GBP-1, GBP-2 and GBP-5) carry a C-terminal CaaX-prenylation signal, which is typical for small GTPases of the Ras family, and increases the membrane affinity of proteins. In this study, we demonstrated that GBP-1, GBP-2 and GBP-5 are prenylated in vivo and that prenylation is required for the membrane association of GBP-1, GBP-2 and GBP-5. Using co-immunoprecipitation, yeast-two-hybrid analysis and fluorescence complementation assays, we showed for the first time that GBPs are able to homodimerize in vivo and that the membrane association of GBPs is regulated by dimerization similarly to dynamin. Interestingly, GBPs could also heterodimerize. This resulted in hierarchical positioning effects on the intracellular localization of the proteins. Specifically, GBP-1 recruited GBP-5 and GBP-2 into its own cellular compartment and GBP-5 repositioned GBP-2. In addition, GBP-1, GBP-2 and GBP-5 were able to redirect non-prenylated GBPs to their compartment in a prenylation-dependent manner. Overall, these findings prove in vivo the ability of GBPs to dimerize, indicate that heterodimerization regulates sub-cellular localization of GBPs and underscore putative membrane-associated functions of this family of proteins.
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Registered trials
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.