ArticleThe Biochemical journal2007
Domain mapping on the human metastasis regulator protein h-Prune reveals a C-terminal dimerization domain.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- PRUNE1 and NME/NDPK family proteins influence energy metabolism and signaling in cancer metastases.Cancer metastasis reviews · 2024Review
- PRUNE1 c.933G>A synonymous variant induces exon 7 skipping, disrupts the DHHA2 domain, and leads to an atypical NMIHBA syndrome presentation: Case report and review of the literature.American journal of medical genetics. Part A · 2022Review
- Functional Genomics of PRUNE1 in Neurodevelopmental Disorders (NDDs) Tied to Medulloblastoma (MB) and Other Tumors.Frontiers in oncology · 2021Review
- Inorganic polyphosphate in platelet rich plasma accelerates re-epithelializationRegenerative therapy · 2020Article
- A competitive cell-permeable peptide impairs Nme-1 (NDPK-A) and Prune-1 interaction: therapeutic applications in cancer.Laboratory investigation; a journal of technical methods and pathology · 2018Review
- A phosphodiesterase 2A isoform localized to mitochondria regulates respiration.The Journal of biological chemistry · 2011Article
- The exopolyphosphatase TbrPPX1 of Trypanosoma brucei.BMC microbiology · 2011Article
- The Nm23-H1-h-Prune complex in cellular physiology: a 'tip of the iceberg' protein network perspective.Molecular and cellular biochemistry · 2009Review
- Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility.Oncogene · 2008Article
- Understanding h-prune biology in the fight against cancer.Clinical & experimental metastasis · 2007Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human orthologue of the Drosophila prune protein (h-Prune) is an interaction partner and regulator of the metastasis suppressor protein NM23-H1 (non-metastatic protein 23). Studies on a cellular breast-cancer model showed that inhibition of the cAMP-specific PDE (phosphodiesterase) activity of h-Prune lowered the incidence of metastasis formation, suggesting that inhibition of h-Prune could be a therapeutic approach towards metastatic tumours. H-Prune shows no sequence similarity with known mammalian PDEs, but instead appears to belong to the DHH (Asp-His-His) superfamily of phosphoesterases. In order to investigate the structure and molecular function of h-Prune, we expressed recombinant h-Prune in a bacterial system. Through sequence analysis and limited proteolysis, we identified domain boundaries and a potential coiled-coil region in a C-terminal cortexillin homology domain. We found that this C-terminal domain mediated h-Prune homodimerization, as well as its interaction with NM23-H1. The PDE catalytic domain of h-Prune was mapped to the N-terminus and shown to be active, even when present in a monomeric form. Our findings indicate that h-Prune is composed of two independent active sites and two interaction sites for the assembly of oligomeric signalling complexes.
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