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Details on Person Guanylate-binding protein 5 (GBP5) is geranylgeranylated at ...
| Class:Id | Summation:9954191 |
|---|---|
| _displayName | Guanylate-binding protein 5 (GBP5) is geranylgeranylated at ... |
| _timestamp | 2026-03-26 20:47:11 |
| created | [InstanceEdit:9954263] Shamovsky, Veronica, 2025-06-06 |
| literatureReference | [LiteratureReference:9953159] Protein prenylation: a pivotal posttranslational process [LiteratureReference:9947919] Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner [LiteratureReference:9953165] Structure of mammalian protein geranylgeranyltransferase type-I [LiteratureReference:9953155] cDNA cloning and expression of rat and human protein geranylgeranyltransferase type-I [LiteratureReference:9954202] Protein prenylation: unique fats make their mark on biology [LiteratureReference:9954247] To finish things well: cysteine methylation ensures selective GTPase membrane localization and signalling |
| modified | [InstanceEdit:9986085] Shamovsky, Veronica, 2026-03-26 |
| text | Guanylate-binding protein 5 (GBP5) is geranylgeranylated at cysteine 583 (C583) within the C-termini CVLL sequence, a CAAX box motif (Britzen-Laurent N et al., 2010). The CAAX box motif, where C = cysteine, A = any aliphatic amino acid, and X = any amino acid, is recognized by geranylgeranyltransferase type I (GGTase I), which covalently attaches a 20-carbon geranylgeranyl isoprenoid group, donated by geranylgeranyl pyrophosphate (GGPP), to the C-terminal cysteine residue of target proteins in a Zn²⁺-dependent manner (reviewed by Roskoski R Jr, 2003). GGTase I functions as a heterodimer composed of an alpha subunit, FNTA (shared with another prenylating enzyme, farnesyltransferase), and a unique beta subunit, PGGT1B (Zhang FL et al., 1994, Taylor JS et al., 2003). This modification enhances GBP5's interaction with membranes. Once prenylated, CAAX-containing proteins undergo proteolytic cleavage of the terminal AAX tripeptide. This reaction is catalyzed by endopeptidases such as RAS-converting enzyme 1 (RCE1), resulting in exposure of the prenylated cysteine as the new C-terminus. The exposed cysteine can then be methylated by isoprenylcysteine carboxyl methyltransferase (ICMT) (reviewed by Wang M & Casey PJ 2016; Cansado J 2018). This sequence of post-translational modifications is considered a common mechanism by which CAAX-containing proteins, including GBP1, GBP2, and GBP5, are activated. However, there is no direct evidence for proteolytic removal of the C-terminal tripeptide or ICMT-mediated methylation of the C-terminal cysteine in GBPs; therefore, these steps are not depicted here. |
| (summation) | [Reaction:9954195] FNTA:PGGT1B geranylgeranylates GBP5 [Homo sapiens] |
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No pathways have been reviewed or authored by Guanylate-binding protein 5 (GBP5) is geranylgeranylated at ... (9954191)
