ARHGEF2
Gene Ontology Biological Process
- actin filament organization [IMP]
- apoptotic signaling pathway [TAS]
- cell morphogenesis [IMP]
- cellular hyperosmotic response [ISS]
- cellular response to muramyl dipeptide [IDA]
- cellular response to tumor necrosis factor [ISS]
- intracellular protein transport [NAS]
- negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [ISS]
- negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress [ISS]
- negative regulation of microtubule depolymerization [IMP]
- negative regulation of necroptotic process [ISS]
- neurotrophin TRK receptor signaling pathway [TAS]
- positive regulation of NF-kappaB transcription factor activity [IDA]
- positive regulation of Rac GTPase activity [IDA]
- positive regulation of Rho GTPase activity [IDA]
- positive regulation of apoptotic process [TAS]
- positive regulation of interleukin-6 production [IDA]
- positive regulation of peptidyl-tyrosine phosphorylation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of tumor necrosis factor production [IDA]
- regulation of Rho protein signal transduction [NAS]
- regulation of cell proliferation [TAS]
- regulation of small GTPase mediated signal transduction [TAS]
- small GTPase mediated signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
DYNLT1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
MARK3-mediated phosphorylation of ARHGEF2 couples microtubules to the actin cytoskeleton to establish cell polarity.
The PAR-1-MARK pathway controls cell polarity through the phosphorylation of microtubule-associated proteins. Rho-Rac guanine nucleotide exchange factor 2 (ARHGEF2), which activates Ras homolog family member A (RHOA), is anchored to the microtubule network and sequestered in an inhibited state through binding to dynein light chain Tctex-1 type 1 (DYNLT1). We showed in mammalian cells that liver kinase B1 (LKB1) activated ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ARHGEF2 DYNLT1 | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| ARHGEF2 DYNLT1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | 2547613 |
Curated By
- BioGRID