GTPase properties of the interferon‐induced human guanylate‐binding protein 2

Neun, Rtidiger; Richter, Marc François; Staeheli, Peter; Schwemmle, Martin

doi:10.1016/0014-5793(96)00628-x

Cited by 51 publications

(36 citation statements)

References 14 publications

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“…(hGBP1 and hGBP2) convert GDP further to GMP (Schwemmle and Staeheli, 1994;Neun et al, 1996;Taylor et al, 1996;Carlow et al, 1998;Han et al, 1998;Uthaiah et al, 2003;Tiwari and MacMicking, unpublished). Two-step hydrolysis is unusual for a G-domain and insights into the reaction mechanism have been obtained from crystal structures of transition-state analog-bound GBP1 (Prakash et al, 2000a, b) and its isolated catalytic region (Ghosh et al, 2006) ( Fig.…”

Section: Stretches and Structuresmentioning

confidence: 95%

Emerging themes in IFN-γ-induced macrophage immunity by the p47 and p65 GTPase families

Shenoy¹,

Kim²,

Choi³

et al. 2008

Immunobiology

119

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Vertebrates have evolved complex immune specificity repertoires beyond the primordial components found in lower multi-cellular organisms to combat microbial infections. The type II interferon (IFN-gamma) pathway represents one such system, bridging innate and acquired immunity and providing host protection in a cell-autonomous manner. Recent large-scale transcriptome analyses of IFN-gamma-dependent gene expression in effector cells such as macrophages have highlighted the prominence of two families of GTPases -- p47 IRGs and p65 GBPs -- that are now beginning to emerge as major determinants of antimicrobial resistance. Here we discuss the recent clarification of known family members, their cellular biochemistry and host defense functions as a means to understanding the complex innate immune response engendered in higher vertebrates such as humans and mice.

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Section: Stretches and Structuresmentioning

confidence: 95%

Emerging themes in IFN-γ-induced macrophage immunity by the p47 and p65 GTPase families

Shenoy¹,

Kim²,

Choi³

et al. 2008

Immunobiology

119

View full text Add to dashboard Cite

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“…2A). The similarity between the predicted three-dimensional structure of AtGC1 and that of the P-loop structure contained in nucleotide triphosphate hydrolases (28,29) is noteworthy, since nucleotide triphosphate hydrolases can convert GTP to both GDP and GMP (30,31). In triphosphate hydrolases, the P-loop interacts with Mg 2ϩ for GTP binding and hydrolysis, and it may be argued that the P-loop-like structure in AtGC1 has an analogous function, and this is supported by the observed dependence of the catalytic activity of AtGC1 on Mg 2ϩ (Fig.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Novel Protein with Guanylyl Cyclase Activity in Arabidopsis thaliana

Ludidi

Gehring

2003

Journal of Biological Chemistry

165

147

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Guanylyl cyclases (GCs) catalyze the formation of the second messenger guanosine 3,5-cyclic monophosphate (cGMP) from guanosine 5-triphosphate (GTP). While many cGMP-mediated processes in plants have been reported, no plant molecule with GC activity has been identified. When the Arabidopsis thaliana genome is queried with GC sequences from cyanobacteria, lower and higher eukaryotes no unassigned proteins with significant similarity are found. However, a motif search of the A. thaliana genome based on conserved and functionally assigned amino acids in the catalytic center of annotated GCs returns one candidate that also contains the adjacent glycine-rich domain typical for GCs. In this molecule, termed AtGC1, the catalytic domain is in the N-terminal part. AtGC1 contains the arginine or lysine that participates in hydrogen bonding with guanine and the cysteine that confers substrate specificity for GTP. When AtGC1 is expressed in Escherichia coli, cell extracts yield >2.5 times more cGMP than control extracts and this increase is not nitric oxide dependent. Furthermore, purified recombinant AtGC1 has Mg 2؉ -dependent GC activity in vitro and >3 times less adenylyl cyclase activity when assayed with ATP as substrate in the absence of GTP. Catalytic activity in vitro proves that AtGC1 can function either as a monomer or homo-oligomer. AtGC1 is thus not only the first functional plant GC but also, due to its unusual domain organization, a member of a new class of GCs.

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“…15,16 GBPs have a concentration-dependent intrinsic high-turnover GTPase activity. [17][18][19] In particular, based on the crystal structure of GBP-1 20,21 and on biochemical considerations, it was proposed that GBP-1 belongs to the group of large GTP-binding proteins such as Mx and dynamin, all of which have a similar domain composition and GTPase activity, although sequence homology is very low. 20 We have shown that GBP-1 is the key and selective mediator of the anti-proliferative effect of ICs on both microvascular and macrovascular endothelial cells in vitro and that GBP-1 expression was inversely related with cell proliferation in vessel endothelial cells of Kaposi's sarcoma (KS) in vivo.…”

Section: During Angiogenesis and Inflammatory Processes Endothelial mentioning

confidence: 99%

Guanylate-Binding Protein-1 Expression Is Selectively Induced by Inflammatory Cytokines and Is an Activation Marker of Endothelial Cells during Inflammatory Diseases

Lubeseder‐Martellato

Guenzi

Jörg

et al. 2002

The American Journal of Pathology

Self Cite

134

140

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During angiogenesis and inflammatory processes, endothelial cells acquire different activation phenotypes, whose identification may help in understanding the complex network of angiogenic and inflammatory interactions in vivo. To this goal we investigated the expression of the human guanylatebinding protein (GBP)-1 that is highly induced by inflammatory cytokines (ICs) and, therefore, may characterize IC-activated cells. Using a new rat monoclonal antibody raised against GBP-1, we show that GBP-1 is a cytoplasmic protein and that its expression in endothelial cells is selectively induced by interferon-␥, interleukin-1␣, interleukin-1␤, or tumor necrosis factor-␣, but not by other cytokines, chemokines, or growth factors. Moreover, we found that GBP-1 expression is highly associated with vascular endothelial cells as confirmed by the simultaneous detection of GBP-1 and the endothelial cell-associated marker CD31 in a broad range of human tissues. Notably, GBP-1 expression was undetectable in the skin, but it was highly induced in vessels of skin diseases with a high-inflammatory component including pso-

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GTPase properties of the interferon‐induced human guanylate‐binding protein 2

Cited by 51 publications

References 14 publications

Emerging themes in IFN-γ-induced macrophage immunity by the p47 and p65 GTPase families

Emerging themes in IFN-γ-induced macrophage immunity by the p47 and p65 GTPase families

Identification of a Novel Protein with Guanylyl Cyclase Activity in Arabidopsis thaliana

Guanylate-Binding Protein-1 Expression Is Selectively Induced by Inflammatory Cytokines and Is an Activation Marker of Endothelial Cells during Inflammatory Diseases

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