The DOI matches its Crossref record, with a small difference in title or year; 3 of the 3 references it cites were found in a registry or an index.
Modulation of Host Signaling by a Bacterial Mimic
Abstract
Salmonella spp. utilize a specialized protein secretion system to deliver a battery of effector proteins into host cells. Several of these effectors stimulate Cdc42- and Rac1-dependent cytoskeletal changes that promote bacterial internalization. These potentially cytotoxic alterations are rapidly reversed by the effector SptP, a tyrosine phosphatase and GTPase activating protein (GAP) that targets Cdc42 and Rac1. The 2.3 A resolution crystal structure of an SptP-Rac1 transition state complex reveals an unusual GAP architecture that mimics host functional homologs. The phosphatase domain possesses a conserved active site but distinct surface properties. Binding to Rac1 induces a dramatic stabilization in SptP of a four-helix bundle that makes extensive contacts with the Switch I and Switch II regions of the GTPase.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Notably, the crystal structure of Rac1 bound to the GAP domain of Salmonella sptP identifies the 4 conserved amino acids, Q61, E62, D63, and Y64, in direct contact with the GAP protein domain, 31 suggesting that mutations at these amino acids could inhibit GAP binding to the activated Rac molecule leading to extended RAC activation.”
From Dominant activating RAC2 mutation with lymphopenia, immunodeficiency, and cytoskeletal defects (2019) · cites this paper as [31]
Citations
Cites
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984 · cited 1×
“The tyrosine of 2.0 Å (210 residues) and 1.8 Å (218 residues), respecphosphatase activity was measured using a tyrosine phosphorytively (Holm and Sander, 1993; Barford et al., 1994;lated peptide derived from human hirudim in the presence and abStuckey et al., 1994).”
MethodInfluentialThe Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants
Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., & Wittinghofer, A. (1997) · Science · doi:10.1126/science.277.5324.333 · Cited by 1,543
A new approach to protein fold recognition
Jones, D. T., Taylort, W. R., & Thornton, J. M. (1992) · Nature · doi:10.1038/358086a0 · Cited by 1,221
Research works printed but not linked: 42
- Abrahams, 1996, Methods used in the structure determination of bovine mitochondiral F1 ATPase, Acta Crystallogr. D, 52, 30, 10.1107/S0907444995008754 · DOI
- Barford, 1994, Crystal structure of human protein tyrosine phosphatase 1B, Science, 263, 1397, 10.1126/science.8128219 · DOI
- Barrett, 1997, The structure of the GTPase-activating domain from p50rhoGAP, Nature, 385, 458, 10.1038/385458a0 · DOI
- Berger, 1995, Predicting coiled coils by use of pairwise residue correlations, Proc. Natl. Acad. Sci. USA, 92, 8259, 10.1073/pnas.92.18.8259 · DOI
- Black, 1997, Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions, EMBO J., 16, 2730, 10.1093/emboj/16.10.2730 · DOI
- Bolin, 1988, The plasmid-encoded Yop2b protein of Yersinia pseudotuberculosis is a virulence determinant regulated by calcium and temperature at the level of transcription, Mol. Microbiol., 2, 237, 10.1111/j.1365-2958.1988.tb00025.x · DOI
- Brunger, 1998, Crystallography & NMR system, Acta Crystallogr. D Biol. Crystallogr., 54, 905, 10.1107/S0907444998003254 · DOI
- Coleman, 1994, Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis, Science, 265, 1405, 10.1126/science.8073283 · DOI
- de La Fortelle, 1997, Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods, Methods Enzymol., 276, 472, 10.1016/S0076-6879(97)76073-7 · DOI
- Finlay, 1997, Common themes in microbial pathogenicity revisited, Microbiol. Mol. Biol. Rev., 61, 136, 10.1128/.61.2.136-169.1997 · DOI
- Fiorentini, 1998, Bacterial toxins and the Rho GTP-binding protein, Cell Death Differ, 5, 720, 10.1038/sj.cdd.4400412 · DOI
- Forsberg, 1990, Genetic analysis of the yopE region of Yersinia spp., J. Bacteriol., 172, 1547, 10.1128/jb.172.3.1547-1555.1990 · DOI
- Fu, 1999, A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion, Nature, 401, 293, 10.1038/45829 · DOI
- Galan, 1999, Interaction of Salmonella with host cells through the centisome 63 type III secretion system, Curr. Opin. Microbiol., 2, 46, 10.1016/S1369-5274(99)80008-3 · DOI
- Galan, 1996, Cross-talk between bacterial pathogens and their host cells, Annu. Rev. Cell Dev. Biol., 12, 219, 10.1146/annurev.cellbio.12.1.221 · DOI
- Galan, 1999, Type III secretion machines, Science, 284, 322, 10.1126/science.284.5418.1322 · DOI
- Goehring, 1999, The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases, J. Biol. Chem., 274, 36369, 10.1074/jbc.274.51.36369 · DOI
- Guex, 1997, SWISS-MODEL and the Swiss-Pdb viewer, Electrophoresis, 18, 2714, 10.1002/elps.1150181505 · DOI
- Hall, 1998, Rho GTPases and the actin cytoskeleton, Science, 279, 509, 10.1126/science.279.5350.509 · DOI
- Hardt, 1998, Salmonella typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells, Cell, 93, 815, 10.1016/S0092-8674(00)81442-7 · DOI
- Hirshberg, 1997, The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue, Nat. Struct. Biol., 4, 147, 10.1038/nsb0297-147 · DOI
- Jones, 1991, Improved methods for binding protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A, 47, 110, 10.1107/S0108767390010224 · DOI
- Kaniga, 1996, A secreted tyrosine phosphatase with modular effector domains encoded by the bacterial pathogen Salmonella typhimurium, Mol. Microbiol., 21, 633, 10.1111/j.1365-2958.1996.tb02571.x · DOI
- Kraulis, 1991, Molscript, J. Appl. Crystallogr., 24, 946, 10.1107/S0021889891004399 · DOI
- Kulich, 1994, Cloning the structural gene for the 49-kDa form of exoenzyme S (exoS) from Pseudomonas aeruginosa strain 388, J. Biol. Chem., 269, 10431, 10.1016/S0021-9258(17)34078-4 · DOI
- Laskowski, 1998, Validation of protein models derived from experiment, Curr. Opin. Struct. Biol., 8, 631, 10.1016/S0959-440X(98)80156-5 · DOI
- Merrit, 1994, Raster3D Version 2.0, Acta Crystallogr. D, 50, 869, 10.1107/S0907444994006396 · DOI
- Michiels, 1988, Nucleotide sequence and transcription analysis of yop51 from Yersinia enterocolitica W22703, Microb. Pathog., 5, 449, 10.1016/0882-4010(88)90006-X · DOI
- Michiels, 1990, Secretion of Yop proteins by Yersiniae, Infect. Immun., 58, 2840, 10.1128/IAI.58.9.2840-2849.1990 · DOI
- Nassar, 1998, Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP, Nat. Struct. Biol., 5, 1047, 10.1038/4156 · DOI
- Otwinowski, 1997, Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol., 276, 307, 10.1016/S0076-6879(97)76066-X · DOI · Paper page
- Pang, 1998, Typhoid fever-important issues still remain, Trends Microbiol., 6, 131, 10.1016/S0966-842X(98)01236-0 · DOI
- Persson, 1997, The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions, EMBO J., 16, 2307, 10.1093/emboj/16.9.2307 · DOI
- Rittinger, 1997, Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue, Nature, 389, 758, 10.1038/39651 · DOI
- Self, 1995, Measurements of intrinsic nucleotide exchange and GTP hydrolysis rates, Meth. Enzymol., 256, 67, 10.1016/0076-6879(95)56010-6 · DOI
- Sondek, 1994, GTPase mechanism of G proteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4, Nature, 372, 276, 10.1038/372276a0 · DOI
- Stender, 2000, Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell, Mol. Microbiol., 36, 1206, 10.1046/j.1365-2958.2000.01933.x · DOI
- Stuckey, 1994, Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate, Nature, 370, 571, 10.1038/370571a0 · DOI
- Takeuchi, 1967, Electron microscopic studies of experimental Salmonella infection. 1. Penetration into the intestinal epithelium by Salmonella typhimurium, Am. J. Pathol., 50, 109
- Van Aelst, 1997, Rho GTPases and signaling networks, Genes Dev., 11, 2295, 10.1101/gad.11.18.2295 · DOI
- Von Pawel-Rammingen, 2000, GAP activity of the Yersinia YopE cytotoxin specifically targets the rho pathway, Mol. Microbiol., 36, 737, 10.1046/j.1365-2958.2000.01898.x · DOI
- Wittinghofer, 1997, Signaling mechanistics, Curr. Biol., 7, R682, 10.1016/S0960-9822(06)00355-1 · DOI
Cited by
The Guanine Nucleotide-Binding Switch in Three Dimensions
Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875
Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE
Buchwald, G., Friebel, A., Galán, J. E., Hardt, W., Wittinghofer, A., & Scheffzek, K. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf329 · Cited by 135
Self-citationDeciphering the Molecular and Functional Basis of Dbl Family Proteins
Jaiswal, M., Dvorsky, R., & Ahmadian, M. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.429746 · Cited by 108
Dominant activating RAC2 mutation with lymphopenia, immunodeficiency, and cytoskeletal defects
Hsu, A. P., Donkó, A., Arrington, M. E., Swamydas, M., Fink, D., Das, A., Escobedo, O., Bonagura, V., Szabolcs, P., Steinberg, H. N., et al. (2019) · Blood · doi:10.1182/blood-2018-11-886028 · Cited by 92
Metadata
- Authors
- Stebbins, C. E., & Galán, J. E.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2000-12
- Volume
- 6
- Issue
- 6
- Pages
- 1449-1460
- ISSN
- 1097-2765
- Cited by
- 160
- References
- 3
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Modulation of Host Signaling by a Bacterial Mimic. https://app.cochat.ai/papers/10.1016/s1097-2765(00)00141-6
- The paper
- Stebbins, C. E., & Galán, J. E. (2000). Modulation of Host Signaling by a Bacterial Mimic. Molecular Cell. https://doi.org/10.1016/s1097-2765(00)00141-6