LIMK1
Gene Ontology Biological Process
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- Rho protein signal transduction [TAS]
- actin cytoskeleton organization [TAS]
- axon guidance [TAS]
- innate immune response [TAS]
- negative regulation of ubiquitin-protein transferase activity [IDA]
- nervous system development [TAS]
- positive regulation of actin filament bundle assembly [IDA]
- positive regulation of axon extension [ISS]
- protein phosphorylation [IDA, IMP]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
LIMK1
Gene Ontology Biological Process
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- Rho protein signal transduction [TAS]
- actin cytoskeleton organization [TAS]
- axon guidance [TAS]
- innate immune response [TAS]
- negative regulation of ubiquitin-protein transferase activity [IDA]
- nervous system development [TAS]
- positive regulation of actin filament bundle assembly [IDA]
- positive regulation of axon extension [ISS]
- protein phosphorylation [IDA, IMP]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Self-association of LIM-kinase 1 mediated by the interaction between an N-terminal LIM domain and a C-terminal kinase domain.
LIM-kinase 1 (LIMK1) and 2 (LIMK2) are members of a novel class of protein kinases containing two LIM motifs at the N-terminus. The LIM motif is thought to be involved in protein-protein interactions. We report here evidence that LIMK1 self-associates and also associates with LIMK2. In vivo and in vitro binding analyses using variously deleted mutants of LIMKI revealed that ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| LIMK1 LIMK1 | 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 | - |
Curated By
- BioGRID