ArticleScientific reports2017
MAPK1 of Leishmania donovani interacts and phosphorylates HSP70 and HSP90 subunits of foldosome complex.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- The atypical dual-specificity protein phosphatase (DUSP)/kinatase of Leishmania infantum modulates infectivity, oxidative stress response and antimonial resistance.PLoS neglected tropical diseases · 2026Article
- Studies Combining Network Pharmacology withCombinatorial chemistry & high throughput screening · 2026Article
- Unraveling the Role of Proteinopathies in Parasitic Infections.Biomedicines · 2025Review
- Genomic Insight of Leishmania Parasite: In-Depth Review of Drug Resistance Mechanisms and Genetic Mutations.ACS omega · 2024Review
- The paradigm of intracellular parasite survival and drug resistance in leishmanial parasite through genome plasticity and epigenetics: Perception and future perspective.Frontiers in cellular and infection microbiology · 2023Review
- Distinguishing functions of trypanosomatid protein kinases.Trends in parasitology · 2022Review
- Promastigote-to-Amastigote Conversion inPathogens (Basel, Switzerland) · 2022Review
- Exploring actinomycetes natural products to identify potential multi-target inhibitors against3 Biotech · 2022Article
- Review
- [Mechanism and material basis ofNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2021Article
- Heat Shock Proteins as the Druggable Targets in Leishmaniasis: Promises and Perils.Infection and immunity · 2021Review
- Casein kinase 1.2 over expression restores stress resistance to Leishmania donovani HSP23 null mutants.Scientific reports · 2020Article
- An overview of biochemically characterized drug targets in metabolic pathways of Leishmania parasite.Parasitology research · 2020Review
- Review
- A BONCAT-iTRAQ method enables temporally resolved quantitative profiling of newly synthesised proteins in Leishmania mexicana parasites during starvation.PLoS neglected tropical diseases · 2019Article
- An Overview of Drug Resistance in Protozoal Diseases.International journal of molecular sciences · 2019Review
- Protein quality control machinery in intracellular protozoan parasites: hopes and challenges for therapeutic targeting.Cell stress & chaperones · 2019Review
- Leishmania donovani 90 kD Heat Shock Protein - Impact of Phosphosites on Parasite Fitness, Infectivity and Casein Kinase Affinity.Scientific reports · 2019Article
- Leishmania phosphatase PP5 is a regulator of HSP83 phosphorylation and essential for parasite pathogenicity.Parasitology research · 2018Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MAP kinases (MAPK) are the most downstream kinases in signal transduction cascades and regulate critical cellular activities such as cell proliferation, differentiation, mortality, stress response, and apoptosis. The Leishmania donovani MAPK1 (LdMAPK1) is involved in parasite viability and drug resistance, but its substrates have not been identified yet. Aiming to identify the possible targets(s) of LdMAPK1, we sought to isolate interacting partners by co-immunoprecipitation, gel electrophoresis and mass spectrometry. Out of fifteen analyzed protein bands, four were identified as subunits of the HSP90 foldosome complex, namely HSP 90, HSP70, STI and SGT. Western blot analysis not only confirmed that LdMAPK1 interacts with HSP70 and HSP90 but also demonstrated that MAPK1 abundance modulates their expression. The interaction is sensitive to treatment with AMTZD, a competitive ERK inhibitor. MAPK1 also displayed kinase activity with HSP90 or HSP70 as substrates. By phosphorylating HSPs in the foldosome complex, MAPK1 may regulate the stability and activity of the foldosome which in turn plays a pivotal role in the parasitic life cycle of L. donovani. Our study therefore implicates LdMAPK1 in the post-translational modification and possibly the regulation of heat shock proteins. Conversely, HSP90 and HSP70 are identified as the first substrates of LdMAPK1.
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