ArticleThe Journal of biological chemistry2009
Domain interplay mediated by an essential disulfide linkage is critical for the activity and secretion of the metastasis-promoting enzyme autotaxin.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- Autotaxin-Lysophosphatidate Axis: Promoter of Cancer Development and Possible Therapeutic Implications.International journal of molecular sciences · 2024Review
- Review
- Review
- Selective export of autotaxin from the endoplasmic reticulum.The Journal of biological chemistry · 2017Article
- Autotaxin, a lysophospholipase D with pleomorphic effects in oncogenesis and cancer progression.Journal of lipid research · 2016Review
- Role of the autotaxin-lysophosphatidate axis in cancer resistance to chemotherapy and radiotherapy.Biochimica et biophysica acta · 2013Review
- Cellular function and molecular structure of ecto-nucleotidases.Purinergic signalling · 2012Review
- Autotaxin: its role in biology of melanoma cells and as a pharmacological target.Enzyme research · 2011Article
- Crystal structure of autotaxin and insight into GPCR activation by lipid mediators.Nature structural & molecular biology · 2011Article
- Location, location, location: a crystal-clear view of autotaxin saturating LPA receptors.Nature structural & molecular biology · 2011Article
- Structural basis of substrate discrimination and integrin binding by autotaxin.Nature structural & molecular biology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Autotaxin or NPP2 (nucleotide pyrophosphatase/phosphodiesterase 2) is a secreted lysophospholipase-D that promotes metastasis and tumor growth by its ability to generate lysophosphatidic acid. Considerable evidence suggests that inhibitors of NPP2 can be used as a novel therapy for the treatment of cancer. Although most attention is currently directed toward the development of inhibitors of the catalytic site, we have explored whether NPP2 can also be targeted through its non-catalytic nuclease-like domain. We demonstrate here that the catalytic and nuclease-like domains are covalently linked by an essential disulfide bridge between Cys(413) and Cys(805). Within the nuclease-like domain, residues 829-850 are involved in the secretion of NPP2, and Lys(852) is required for the expression of catalytic activity. These data show that the nuclease-like domain is crucial for catalysis by NPP2 and is a possible target to generate inhibitors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.