The Guanylate-Binding Proteins: Emerging Insights into the Biochemical Properties and Functions of This Family of Large Interferon-Induced Guanosine Triphosphatase
| Autor: | Deborah J. Vestal, Jonathan A. Jeyaratnam |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Immunology
Protein Prenylation Guanosine Reviews Endothelial Cells Cell Biology GTPase Guanosine triphosphate Biology Gene Expression Regulation Enzymologic chemistry.chemical_compound GTP-binding protein regulators chemistry Biochemistry Guanosine diphosphate GTP-Binding Proteins Virology Multigene Family Guanosine monophosphate Animals Humans Triphosphatase Protein Interaction Domains and Motifs Guanine nucleotide exchange factor Interferons |
| Popis: | Originally identified by their unusual ability to bind guanosine monophosphate (GMP) nucleotide agarose, the guanylate-binding proteins (GBPs) were used extensively to promote our understanding of interferon-induced gene transcription and as markers of interferon responsiveness. Structural and biochemical analyses of human GBP-1 subsequently demonstrated that the GBPs are a unique subfamily of guanosine triphosphatase (GTPases) that hydrolyze guanosine triphosphate (GTP) to both guanosine diphosphate (GDP) and GMP. As members of the larger dynamin superfamily of GTPases, GBPs exhibit such properties as nucleotide-dependent oligomerization and concentration-dependent GTPase activity. Recently, progress has been made in assigning functions to members of the GBP family. While many of these functions involve protection against intracellular pathogens, a growing number of them are not directly related to pathogen protection. It is currently unclear how the unusual properties of GBPs contribute to this growing list of functions. As future studies uncover the molecular mechanism(s) of action of the GBPs, we will gain a greater understanding of how individual GBPs can mediate what currently appears to be a divergent set of functions. |
| Databáze: | OpenAIRE |
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