ReviewFunctional & integrative genomics2012
Prediction of biological functions of Shewanella-like protein phosphatases (Shelphs) across different domains of life.
Review in Functional & integrative genomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Linear motifs regulating protein secretion, sorting and autophagy in Leishmania parasites are diverged with respect to their host equivalents.PLoS computational biology · 2024Article
- Parasite protein phosphatases: biological function, virulence, and host immune evasion.Parasitology research · 2021Review
- Shelph2, a bacterial-like phosphatase of the malaria parasite Plasmodium falciparum, is dispensable during asexual blood stage.PloS one · 2017Article
- Genome wide in silico analysis of Plasmodium falciparum phosphatome.BMC genomics · 2014Article
- Evolution of bacterial-like phosphoprotein phosphatases in photosynthetic eukaryotes features ancestral mitochondrial or archaeal origin and possible lateral gene transfer.Plant physiology · 2013Article
- An ancient protein phosphatase, SHLP1, is critical to microneme development in Plasmodium ookinetes and parasite transmission.Cell reports · 2013Article
- A unique protein phosphatase with kelch-like domains (PPKL) in Plasmodium modulates ookinete differentiation, motility and invasion.PLoS pathogens · 2012Article
- Okadaic acid and microcystin insensitive PPP-family phosphatases may represent novel biotechnology targets.Plant signaling & behavior · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PPP protein phosphatases are an important enzyme family involved in a variety of aspects of cellular signalling and metabolism. PPPs are ubiquitous in eukaryotes, and are also present in many bacteria. Canonical eukaryotic PPP phosphotases are represented by five major subfamilies (PP1, PP2A, calcineurin, PP5 and PPEF/PP7). We previously reported that three "bacterial-like" PPP groups span the prokaryote-eukaryote boundary, including "Shewanella-like" phosphatases (Shelphs), which are in the focus of this study. Here we predict possible biological functions and functional partners of Shelphs by examining composition of bacterial operons and expression data for eukaryotes available in public databases. In Arabidopsis thaliana, the predicted possible roles include light-dependent regulation of chloroplast functions, signalling between the nucleus and the chloroplast, and defence responses. In Plasmodium falciparum, Shelphs are predicted to be associated with host cell invasion. One isoform has been located in the apical complex, essential for the interaction with the host cell. This makes P. falciparum Shelphs obvious potential candidates for therapeutic targets. Shelphs are also present in bacteria that constitute a considerable proportion of symbiotic microflora in humans. The predicted involvement of bacterial Shelphs in sensing and import of nutrients and extrusion of toxins may be relevant to the links between physiology of humans and our symbionts. Thus, despite the absence of Shelphs in animals, including humans, they may have a direct relationship to human health. Some predicted biological processes and potential functional partners of Shelphs are common between different bacterial and/or eukaryotic lineages, suggesting evolutionary conservation of some Shelph regulatory modules.
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