BioGPS: an extensible and customizable portal for querying and organizing gene annotation resources

Wu, Chunlei; Orozco, Camilo Alberto Madariaga; Boyer, Jason; Leglise, Marc; Goodale, James; Batalov, Serge; Hodge, Christopher L; Haase, J.; Janes, Jeff; Huss, Jon W.; Su, Andrew I.

doi:10.1186/gb-2009-10-11-r130

Cited by 1,256 publications

(1,305 citation statements)

References 25 publications

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“…6). Gpr111 was mainly expressed in skin and heart, and very weakly in lung and spleen, which is consistent with large-scale microarray datasets (Wu et al, 2009). To corroborate receptor expression within these tissues, Gpr111 LacZ/LacZ mice were stained with X-Gal.…”

Section: Gpr111 and Gpr115 Are Expressed In Squamous Epitheliasupporting

confidence: 86%

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Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

Prömel

Waller-Evans

Dixon

et al. 2012

Developmental Dynamics

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Background: Adhesion G protein-coupled receptors (aGPCR) constitute a structurally and functionally diverse class of seven-transmembrane receptor proteins. Although for some of the members important roles in immunology, neurology, as well as developmental biology have been suggested, most receptors have been poorly characterized. Results: We have studied evolution, expression, and function of an entire receptor group containing four uncharacterized aGPCR: Gpr110, Gpr111, Gpr115, and Gpr116. We show that the genomic loci of these four receptors are clustered tightly together in mouse and human genomes and that this cluster likely derives from a single common ancestor gene. Using transcriptional profiling on wild-type and knockout/LacZ reporter knockin mice strains, we have obtained detailed expression maps that show ubiquitous expression of Gpr116, co-expression of Gpr111 and Gpr115 in developing skin, and expression of Gpr110 in adult kidney. Loss of Gpr110, Gpr111, or Gpr115 function did not result in detectable defects, indicating that genes of this aGPCR group might function redundantly. Conclusions: The aGPCR cluster Gpr110, Gpr111, Gpr115, and Gpr116 developed from one common ancestor in vertebrates. Expression suggests a role in epithelia, and one can speculate about a possible redundant function of GPR111 and GPR115. Developmental Dynamics 241:1591-1602, 2012.V C 2012 Wiley Periodicals, Inc.

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Section: Gpr111 and Gpr115 Are Expressed In Squamous Epitheliasupporting

confidence: 86%

“…Previous transcriptional profiling indicated that Gpr116 is expressed in lung, placenta, heart, and eyecup, whereas Gpr110 transcript was found in cornea, liver, and ciliary bodies (Wu et al, 2009).…”

Section: Gpr116 Is Ubiquitously Expressed and Gpr110 Is Expressed Inmentioning

confidence: 99%

Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

Prömel

Waller-Evans

Dixon

et al. 2012

Developmental Dynamics

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“…Indeed, it is conceivable that cGASexpressing cells generate cGAMP and provide it in trans to STING-expressing, but cGAS-incompetent cells, further amplifying antiviral gene expression in the context of TREX1 deficiency. In line with this concept, it is interesting to note that human cGAS and STING do not follow a tight coexpression pattern across different cell types, with cGAS showing a far more restricted expression pattern than STING (19)(20)(21). On a similar note, it is also possible that differential expression of connexins contributes to the unique confinement of disease activity to distinct tissues in the context of TREX1 deficiency.…”

Section: Discussionmentioning

confidence: 85%

TREX1 Deficiency Triggers Cell-Autonomous Immunity in a cGAS-Dependent Manner

Ablasser

Hemmerling

Schmid-Burgk

et al. 2014

The Journal of Immunology

224

158

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Cytosolic detection of DNA is crucial for the initiation of antiviral immunity but can also cause autoimmunity in the context of endogenous nucleic acids being sensed. Mutations in the human 3′ repair exonuclease 1 (TREX1) have been linked to the type I IFN–associated autoimmune disease Aicardi–Goutières syndrome. The exact mechanisms driving unabated type I IFN responses in the absence of TREX1 are only partly understood, but it appears likely that accumulation of endogenous DNA species triggers a cell-autonomous immune response by activating a cytosolic DNA receptor. In this article, we demonstrate that knocking out the DNA sensor cyclic GMP–AMP synthase completely abrogates spontaneous induction of IFN-stimulated genes in TREX1-deficient cells. These findings indicate a key role of cyclic GMP–AMP synthase for the initiation of self-DNA–induced autoimmune disorders, thus providing important implications for novel therapeutic approaches.

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“…25 Four AAC isoforms have been identified in human with distinct expression patterns. 26,27 According to previous reports, [28][29][30] AAC2 and AAC3 are the dominant AACs in ECs. Co-IP confirmed that ISM interacts with AAC2/AAC3 (Figure 5a).…”

Section: Resultsmentioning

confidence: 93%

Isthmin targets cell-surface GRP78 and triggers apoptosis via induction of mitochondrial dysfunction

Zhang

et al. 2014

Cell Death Differ

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Isthmin (ISM) is a secreted 60-kDa protein that potently induces endothelial cell (EC) apoptosis. It suppresses tumor growth and angiogenesis in mice when stably overexpressed in cancer cells. Although avb5 integrin serves as a low-affinity receptor for ISM, the mechanism by which ISM mediates antiangiogenesis and apoptosis in ECs remain to be fully resolved. In this work, we report the identification of cell-surface glucose-regulated protein 78 kDa (GRP78) as a high-affinity receptor for ISM (K d ¼ 8.6 nM). We demonstrated that ISM-GRP78 interaction triggers apoptosis not only in activated ECs but also in cancer cells expressing high level of cell-surface GRP78. Normal cells and benign tumor cells tend to express low level of cell-surface GRP78 and are resistant to ISM-induced apoptosis. Upon binding to GRP78, ISM is internalized into ECs through clathrin-dependent endocytosis that is essential for its proapoptotic activity. Once inside the cell, ISM co-targets with GRP78 to mitochondria where it interacts with ADP/ATP carriers on the inner membrane and blocks ATP transport from mitochondria to cytosol, thereby causing apoptosis. Hence, ISM is a novel proapoptotic ligand that targets cell-surface GRP78 to trigger apoptosis by inducing mitochondrial dysfunction. The restricted and high-level expression of cell-surface GRP78 on cancer cells and cancer ECs make them uniquely susceptible to ISM-targeted apoptosis. Indeed, systemic delivery of recombinant ISM potently suppressed subcutaneous 4T1 breast carcinoma and B16 melanoma growth in mice by eliciting apoptosis selectively in the cancer cells and cancer ECs. Together, this work reveals a novel ISM-GRP78 apoptosis pathway and demonstrates the potential of ISM as a cancer-specific and dual-targeting anticancer agent.

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BioGPS: an extensible and customizable portal for querying and organizing gene annotation resources

Abstract: BioGPS is a community based customisable gene annotation portal bringing together gene annotation resources on to a single platform.

Cited by 1,256 publications

References 25 publications

Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

TREX1 Deficiency Triggers Cell-Autonomous Immunity in a cGAS-Dependent Manner

Isthmin targets cell-surface GRP78 and triggers apoptosis via induction of mitochondrial dysfunction

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