ArticleThe Journal of biological chemistry2010
Structure of Shigella IpgB2 in complex with human RhoA: implications for the mechanism of bacterial guanine nucleotide exchange factor mimicry.
Article in The Journal of biological chemistry, 2010. 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, 56 citations in OpenAlex.
- Mechanistic insights on spatiotemporal control of Ras-signaling.Biological chemistry · 2026Review
- ThemSphere · 2025Article
- Molecular mechanisms of co-infections.EMBO reports · 2025Review
- The Human-Specific miR-6762-5p Is an Activator of RhoA GTPase Enhancing Shigella flexneri Intercellular Spreading.Molecular microbiology · 2025Article
- Conformational Insights into the Control of CNF1 Toxin Activity by Peptidyl-Prolyl Isomerization: A Molecular Dynamics Perspective.International journal of molecular sciences · 2021Article
- α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles.International journal of molecular sciences · 2021Review
- Actin dynamics in host-pathogen interaction.FEBS letters · 2018Review
- Article
- How Do the Virulence Factors ofFrontiers in cellular and infection microbiology · 2017Review
- Bacterial recognition pathways that lead to inflammasome activation.Immunological reviews · 2015Review
- Molecular mechanisms of host cytoskeletal rearrangements by Shigella invasins.International journal of molecular sciences · 2014Review
- A recurrent inactivating mutation in RHOA GTPase in angioimmunoblastic T cell lymphoma.Nature genetics · 2014Article
- Bacterial factors exploit eukaryotic Rho GTPase signaling cascades to promote invasion and proliferation within their host.Small GTPases · 2014Review
- Article
- The inside story of Shigella invasion of intestinal epithelial cells.Cold Spring Harbor perspectives in medicine · 2013Review
- Migration of turkey muscle satellite cells is enhanced by the syndecan-4 cytoplasmic domain through the activation of RhoA.Molecular and cellular biochemistry · 2013Article
- Subversion of cell signaling by pathogens.Cold Spring Harbor perspectives in biology · 2012Review
- Mimicking GEFs: a common theme for bacterial pathogens.Cellular microbiology · 2012Review
- Manipulation of host membranes by bacterial effectors.Nature reviews. Microbiology · 2011Review
- Bacterial protein toxins that modify host regulatory GTPases.Nature reviews. Microbiology · 2011Review
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Authors and funding
8 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A common theme in bacterial pathogenesis is the manipulation of eukaryotic cells by targeting the cytoskeleton. This is in most cases achieved either by modifying actin, or indirectly via activation of key regulators controlling actin dynamics such as Rho-GTPases. A novel group of bacterial virulence factors termed the WXXXE family has emerged as guanine nucleotide exchange factors (GEFs) for these GTPases. The precise mechanism of nucleotide exchange, however, has remained unclear. Here we report the structure of the WXXXE-protein IpgB2 from Shigella flexneri and its complex with human RhoA. We unambiguously identify IpgB2 as a bacterial RhoA-GEF and dissect the molecular mechanism of GDP release, an essential prerequisite for GTP binding. Our observations uncover that IpgB2 induces conformational changes on RhoA mimicking DbI- but not DOCK family GEFs. We also show that dissociation of the GDP.Mg(2+) complex is preceded by the displacement of the metal ion to the alpha-phosphate of the nucleotide, diminishing its affinity to the GTPase. These data refine our understanding of the mode of action not only of WXXXE GEFs but also of mammalian GEFs of the DH/PH family.
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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.