Target type: molecularfunction
The binding activity of a molecule that brings together a guanyl-nucleotide exchange factor and one or more other proteins, permitting them to function in a coordinated way. [GOC:mtg_MIT_16mar07, GOC:vw]
Guanyl-nucleotide exchange factor (GEF) adaptor activity plays a crucial role in regulating the activity of small GTPases, a family of proteins involved in a wide range of cellular processes. GEFs act as molecular switches, catalyzing the exchange of GDP (guanosine diphosphate) for GTP (guanosine triphosphate) on their target GTPases. This exchange event activates the GTPase, enabling it to interact with downstream effectors and initiate signaling cascades.
GEFs themselves are often regulated by upstream signaling pathways, ensuring that GTPase activation occurs in a controlled and context-specific manner. In the context of GEF adaptor activity, the GEF protein acts as a bridge between upstream signaling molecules and the target GTPase. This adaptor function allows for precise control of GTPase activation, ensuring that the appropriate GTPase is activated at the right time and place.
For example, GEF adaptors can interact with scaffolding proteins, which organize signaling complexes and bring together different components of a signaling pathway. This interaction can bring the GEF into close proximity with its target GTPase, facilitating efficient nucleotide exchange. Additionally, GEF adaptors may be regulated by post-translational modifications, such as phosphorylation or ubiquitination, which can alter their activity or localization.
The molecular mechanisms underlying GEF adaptor activity can vary depending on the specific GEF and GTPase involved. However, a common theme is the ability of the GEF to bind both the GTPase and an upstream signaling molecule, effectively acting as a conduit for signal transduction. This adaptor function is essential for the proper regulation of GTPase activity and the downstream signaling events they control.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Growth factor receptor-bound protein 2 | A growth factor receptor-bound protein 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P62993] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| phosphotyrosine | O(4)-phospho-L-tyrosine : A non-proteinogenic L-alpha-amino acid that is L-tyrosine phosphorylated at the phenolic hydroxy group. Phosphotyrosine: An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis. | L-tyrosine derivative; non-proteinogenic L-alpha-amino acid; O(4)-phosphotyrosine | Escherichia coli metabolite; immunogen |
| dactinomycin | Dactinomycin: A compound composed of a two CYCLIC PEPTIDES attached to a phenoxazine that is derived from STREPTOMYCES parvullus. It binds to DNA and inhibits RNA synthesis (transcription), with chain elongation more sensitive than initiation, termination, or release. As a result of impaired mRNA production, protein synthesis also declines after dactinomycin therapy. (From AMA Drug Evaluations Annual, 1993, p2015) | actinomycin | mutagen |
| 7-hydroxycoumarin-4-acetic acid | 7-hydroxycoumarin-4-acetic acid: pH-indicator dye; structure in first source |