ArticleMicrobes and infection2010
Protein kinase A catalytic subunit interacts and phosphorylates members of trans-sialidase super-family in Trypanosoma cruzi.
Article in Microbes and infection, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Prioritization of chemical scaffolds using the TDR Targets database: An integrative workflow for Trypanosoma cruzi drug discovery.PLoS neglected tropical diseases · 2026Article
- Beyond the catalysis of Trypanosoma cruzi trans-sialidases: structure, function, post-translational modifications, intrinsically disordered regions and use of CRISPR/Cas9.Archives of microbiology · 2026Review
- Article
- Signaling pathways involved in environmental sensing in Trypanosoma cruzi.Molecular microbiology · 2021Review
- Large-Scale Phylogenetic Analysis of Trypanosomatid Adenylate Cyclases Reveals Associations with Extracellular Lifestyle and Host-Pathogen Interplay.Genome biology and evolution · 2020Article
- Methods to Investigate Signal Transduction Pathways in Trypanosoma cruzi: Cyclic Nucleotide Phosphodiesterases Assay Protocols.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Quantitative phosphoproteome and proteome analyses emphasize the influence of phosphorylation events during the nutritional stress of Trypanosoma cruzi: the initial moments of in vitro metacyclogenesis.Cell stress & chaperones · 2019Article
- Reprogramming of Trypanosoma cruzi metabolism triggered by parasite interaction with the host cell extracellular matrix.PLoS neglected tropical diseases · 2019Article
- A Multilayer Network Approach for Guiding Drug Repositioning in Neglected Diseases.PLoS neglected tropical diseases · 2016Article
- cAMP signalling in trypanosomatids: role in pathogenesis and as a drug target.Trends in parasitology · 2015Review
- Down regulation of NO signaling in Trypanosoma cruzi upon parasite-extracellular matrix interaction: changes in protein modification by nitrosylation and nitration.PLoS neglected tropical diseases · 2015Article
- The ever unfolding story of cAMP signaling in trypanosomatids: vive la difference!Frontiers in pharmacology · 2015Review
- Kinetoplastid Specific RNA-Protein Interactions in Trypanosoma cruzi Ribosome Biogenesis.PloS one · 2015Article
- Quantitative proteomic and phosphoproteomic analysis of Trypanosoma cruzi amastigogenesis.Molecular & cellular proteomics : MCP · 2014Article
- Identification of novel cyclic nucleotide binding proteins in Trypanosoma cruzi.Molecular and biochemical parasitology · 2014Article
- New insights on the sialidase protein family revealed by a phylogenetic analysis in metazoa.PloS one · 2012Article
- Identification of Toxoplasma gondii cAMP dependent protein kinase and its role in the tachyzoite growth.PloS one · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Protein kinase A (PKA) has been suggested as a regulator of stage differentiation in Trypanosoma cruzi. Using a yeast two-hybrid system we have begun to characterize the downstream substrates of T. cruzi PKA. We identified several members of the trans-sialidase super family by this approach. Immunoprecitation demonstrated that a TcPKAc monoclonal antibody was able to pull-down proteins recognized by trans-sialidase antibodies as well as a SA85-1.1 antibody and vice versa. An in vitro phosphorylation assay demonstrated that PKA phosphorylated the recombinant protein of an active trans-sialidase. In addition, a phospho-(Ser/Thr) PKA substrate antibody detected bands on immunoblot analysis of trans-sialidase antibody precipitated proteins from parasite lysate and the media of L(6)E(9) myoblasts infected with trypomastigotes as well as from a SA85-1.1 antibody precipitated proteins from parasite lysate. Immunofluorescence analysis suggested that some TcPKAc localizes to the plasma membrane surface of trypomastigotes. The identified trans-sialidases have PKA consensus phosphorylation sites located near the endoplasmic reticulum retention motif in the N-terminal. These data support that PKA phosphorylates trans-sialidase super family members in vivo.
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