Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The Campylobacter jejuni CiaD effector co-opts the host cell protein IQGAP1 to promote cell entry

ABSTRACT: Proteomic data from pulldown performed with the recombinant Campylobacter CiaD-GST fusion was expressed in E. coli BL21(DE3) on a lysate of human cultured INT 407 cells. One non-specific binding control was performed on INT 407 cell lysates and two-pulldowns were realized with the recombinant protein. Samples were digested with trypsin, then analyzed by LC-MS/MS. Data was searched with MS-GF+ using PNNL's DMS processing pipeline.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Geremy Clair

PROVIDER: MSV000086662 | MassIVE | Tue Jan 05 10:43:00 GMT 2021

SECONDARY ACCESSION(S): PXD023421

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Publications

The Campylobacter jejuni CiaD effector co-opts the host cell protein IQGAP1 to promote cell entry.

Negretti Nicholas M NM Gourley Christopher R CR Talukdar Prabhat K PK Clair Geremy G Klappenbach Courtney M CM Lauritsen Cody J CJ Adkins Joshua N JN Konkel Michael E ME

Nature communications 20210226 1

Campylobacter jejuni is a foodborne pathogen that binds to and invades the epithelial cells lining the human intestinal tract. Maximal invasion of host cells by C. jejuni requires cell binding as well as delivery of the Cia proteins (Campylobacter invasion antigens) to the host cell cytosol via the flagellum. Here, we show that CiaD binds to the host cell protein IQGAP1 (a Ras GTPase-activating-like protein), thus displacing RacGAP1 from the IQGAP1 complex. This, in turn, leads to the unconstrai ...[more]

PMID: 33637714

Similar Datasets

The Campylobacter jejuni CiaD effector co-opts the host cell protein IQGAP1 to promote cell entry.

Project description:Campylobacter jejuni is a foodborne pathogen that binds to and invades the epithelial cells lining the human intestinal tract. Maximal invasion of host cells by C. jejuni requires cell binding as well as delivery of the Cia proteins (Campylobacter invasion antigens) to the host cell cytosol via the flagellum. Here, we show that CiaD binds to the host cell protein IQGAP1 (a Ras GTPase-activating-like protein), thus displacing RacGAP1 from the IQGAP1 complex. This, in turn, leads to the unconstrained activity of the small GTPase Rac1, which is known to have roles in actin reorganization and internalization of C. jejuni. Our results represent the identification of a host cell protein targeted by a flagellar secreted effector protein and demonstrate that C. jejuni-stimulated Rac signaling is dependent on IQGAP1.

| S-EPMC7910587 | biostudies-literature

Identification of novel RHOA interacting patners

Project description:RHO subfamily of small GTPases comprise highly conserved family members RHOA, RHOB, and RHOC which cycle between GTP-bound 'active' and GDP-bound 'inactive' states. In the active form, RHO proteins interact with a variety of downstream effector proteins, controlling their activity and function. Many of the RHO subfamily effector proteins such as ROCK, PKN, and mDIA, are key regulators of actin cytoskeleton and cell motility. To identify novel effector proteins for RHOA,we carried out a GST-pulldown from heavy or light SILAC labelled HeLa cells using GST tagged GTP-bound RHOA, or GST alone control, as bait. Pulldowns were performed in duplicates with switched labellings. Specific interactors were destinguished from the background on the basis of SILAC Heavy to Light ratios between GST-RHOA and GST alone pulldowns.

2016-11-01 | PXD004934 | Pride

Identification of SOX2-bound mRNA

Project description:In vitro pull down assay was performed using recombinant GST and GST fusion SOX2 protein to precipitate total RNA from urothelial carcinoma cell line BFTC905 Unbound RNA from both reactions and matrix-associated RNA from SOX2 pull down reaction was extracted using TRIZOL reagent

2011-10-26 | GSE33207 | GEO

IQGAP1 is a novel phosphatidylinositol 4,5 bisphosphate effector in regulation of directional cell migration.

Project description:Phosphatidylinositol 4,5 bisphosphate (PIP?) is a key lipid messenger for regulation of cell migration. PIP? modulates many effectors, but the specificity of PIP? signalling can be defined by interactions of PIP?-generating enzymes with PIP? effectors. Here, we show that type I? phosphatidylinositol 4-phosphate 5-kinase (PIPKI?) interacts with the cytoskeleton regulator, IQGAP1, and modulates IQGAP1 function in migration. We reveal that PIPKI? is required for IQGAP1 recruitment to the leading edge membrane in response to integrin or growth factor receptor activation. Moreover, IQGAP1 is a PIP? effector that directly binds PIP? through a polybasic motif and PIP? binding activates IQGAP1, facilitating actin polymerization. IQGAP1 mutants that lack PIPKI? or PIP? binding lose the ability to control directional cell migration. Collectively, these data reveal a synergy between PIPKI? and IQGAP1 in the control of cell migration.

| S-EPMC3791370 | biostudies-literature

Gastric hyperplasia in mice lacking the putative Cdc42 effector IQGAP1.

Project description:Human IQGAP1 is a widely expressed 190-kDa Cdc42-, Rac1-, and calmodulin-binding protein that interacts with F-actin in vivo and that can cross-link F-actin microfilaments in vitro. Recent results have implicated IQGAP1 as a component of pathways via which Cdc42 or Rac1 modulates cadherin-based cell adhesion (S. Kuroda et al., Science 281:832-835, 1998), whereas yeast IQGAP-related proteins have been found to play essential roles during cytokinesis. To identify critical in vivo functions of IQGAP1, we generated deficient mice by gene targeting. We demonstrate that IQGAP1 null mutants arise at normal frequency and show no obvious defects during development or for most of their adult life. Loss of IQGAP1 also does not affect tumor development or tumor progression, but mutant mice exhibit a significant (P < 0.0001) increase in late-onset gastric hyperplasia relative to wild-type animals of the same genetic background. While we cannot exclude that functional redundancy with IQGAP2 contributes to the lack of developmental phenotypes, the restricted expression pattern of IQGAP2 is not obviously altered in adult IQGAP1 mutant mice. Thus, IQGAP1 does not serve any essential nonredundant functions during murine development but may serve to maintain the integrity of the gastric mucosa in older animals.

| S-EPMC85173 | biostudies-literature

Positive role of IQGAP1, an effector of Rac1, in actin-meshwork formation at sites of cell-cell contact.

Project description:The small guanosine triphosphatase Rac1 is activated by E-cadherin-mediated cell-cell adhesion and is required for the accumulation of actin filaments, E-cadherin, and beta-catenin at sites of cell-cell contact. However, the modes of activation and action of Rac1 remain to be clarified. We here found that suppression of IQGAP1, an actin-binding protein and an effector of Rac1, by small interfering RNA apparently reduced the accumulation of actin filaments, E-cadherin, and beta-catenin at sites of cell-cell contact in Madin-Darby canine kidney II epithelial cells under the conditions in which knockdown of Rac1 reduced them. Knockdown of Rac1 did not affect the localization of these junctional components in cells expressing a constitutively active IQGAP1 mutant defective in Rac1/Cdc42 binding. Knockdown of either Rac1 or IQGAP1 accelerated the 12-O-tetradecanoylphorbol-13-acetate-induced cell-cell dissociation. The basal Rac1 activity, which was maintained by E-cadherin-mediated cell-cell adhesion, was inhibited in the IQGAP1-knocked down cells, whereas the Rac1 activity was increased in the cells overexpressing IQGAP1. Together, these results indicate that Rac1 enhances the accumulation of actin filaments, E-cadherin, and beta-catenin by acting on IQGAP1 and suggest that there exists a positive feedback loop comprised of "E-cadherin-mediated cell-cell adhesion --> Rac1 activation --> actin-meshwork formation by IQGAP1 --> increasing E-cadherin-mediated cell-cell adhesion."

| S-EPMC363077 | biostudies-literature

Shigella Effector OspB Activates mTORC1 in a Manner That Depends on IQGAP1 and Promotes Cell Proliferation.

Project description:The intracellular bacterial pathogen Shigella infects and spreads through the human intestinal epithelium. Effector proteins delivered by Shigella into cells promote infection by modulating diverse host functions. We demonstrate that the effector protein OspB interacts directly with the scaffolding protein IQGAP1, and that the absence of either OspB or IQGAP1 during infection leads to larger areas of S. flexneri spread through cell monolayers. We show that the effect on the area of bacterial spread is due to OspB triggering increased cell proliferation at the periphery of infected foci, thereby replacing some of the cells that die within infected foci and restricting the area of bacterial spread. We demonstrate that OspB enhancement of cell proliferation results from activation of mTORC1, a master regulator of cell growth, and is blocked by the mTORC1-specific inhibitor rapamycin. OspB activation of mTORC1, and its effects on cell proliferation and bacterial spread, depends on IQGAP1. Our results identify OspB as a regulator of mTORC1 and mTORC1-dependent cell proliferation early during S. flexneri infection and establish a role for IQGAP1 in mTORC1 signaling. They also raise the possibility that IQGAP1 serves as a scaffold for the assembly of an OspB-mTORC1 signaling complex.

| S-EPMC4608727 | biostudies-literature

TRIM56 acts through the IQGAP1-CDC42 signaling axis to promote glioma cell migration and invasion.

Project description:Diffuse invasion is an important factor leading to treatment resistance and a poor prognosis in gliomas. Herein, we found that expression of the tripartite motif containing 56 (TRIM56), a RING-finger domain containing E3 ubiquitin ligase, was markedly higher in glioma than in normal brain tissue, and was significantly correlated with malignant phenotypes and a poor prognosis. In vitro and in vivo experimental studies revealed that TRIM56 promoted the migration and invasion of glioma cells. Mechanistically, TRIM56 was transcriptionally regulated by SP1 and promoted the K48-K63-linked poly-ubiquitination transition of IQGAP1 at Lys-1230 by interacting with it, which in turn promoted CDC42 activation. This mechanism was confirmed to mediate glioma migration and invasion. In conclusion, our study provides insights into the mechanisms through which TRIM56 promotes glioma motility, i.e., by regulating IQGAP1 ubiquitination to promote CDC42 activation, which might be clinically targeted for the treatment of glioma.

| S-EPMC9985612 | biostudies-literature

Identification of SOX2-bound mRNA

2011-10-25 | E-GEOD-33207 | biostudies-arrayexpress

MYC Mediates mRNA Cap Methylation of Canonical Wnt/beta-catenin Signaling Transcripts by Recruiting CDK7 and RNA Methyltransferase

Project description:We performed an RNA pulldown against a methyl group on the mRNA cap using a fusion protein, GST-eIF4E, highly specific for a m7G-mRNA cap. We performed RNA-seq on both the pulldowns and inputs and normalized our pulldown to input in order to determine which genes MYC targets for mRNA cap methylation above and beyond any affect at the transcriptional level. We found that MYC targets approximately 30% of transcripts for enhanced mRNA cap methylation above 1.2 fold on a global scale following 24 h of MYC induction, specifically transcripts involved in the canonical Wnt/β-catenin signaling pathway. We used this dataset to validate transcripts targeted by MYC for mRNA cap methylation and to help us determine the mechanism responsible for this phenomenon.

2017-01-06 | GSE76614 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data