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Full-Text Articles in Cell and Developmental Biology
Regulation Of Stress-Inducible Phosphoprotein 1 Nuclear Retention By Protein Inhibitor Of Activated Stat Pias1, Iaci N. Soares, Fabiana A. Caetano, Jordan Pinder, Bruna Roz Rodrigues, Flavio H. Beraldo, Valeriy G. Ostapchenko, Chantal Durette, Grace Schenatto Pereira, Marilene H. Lopes, Nicolle Queiroz-Hazarbassanov, Isabela W. Cunha, Paulo I. Sanematsu, Sergio Suzuki, Luiz F. Bleggi-Torres, Caroline Schild-Poulter, Pierre Thibault, Graham Dellaire, Vilma R. Martins, Vania F. Prado, Marco A. M. Prado
Regulation Of Stress-Inducible Phosphoprotein 1 Nuclear Retention By Protein Inhibitor Of Activated Stat Pias1, Iaci N. Soares, Fabiana A. Caetano, Jordan Pinder, Bruna Roz Rodrigues, Flavio H. Beraldo, Valeriy G. Ostapchenko, Chantal Durette, Grace Schenatto Pereira, Marilene H. Lopes, Nicolle Queiroz-Hazarbassanov, Isabela W. Cunha, Paulo I. Sanematsu, Sergio Suzuki, Luiz F. Bleggi-Torres, Caroline Schild-Poulter, Pierre Thibault, Graham Dellaire, Vilma R. Martins, Vania F. Prado, Marco A. M. Prado
Anatomy and Cell Biology Publications
Stress-inducible phosphoprotein 1 (STI1), a cochaperone for Hsp90, has been shown to regulate multiple pathways in astrocytes, but its contributions to cellular stress responses are not fully understood. We show that in response to irradiation-mediated DNA damage stress STI1 accumulates in the nucleus of astrocytes. Also, STI1 haploinsufficiency decreases astrocyte survival after irradiation. Using yeast two-hybrid screenings we identified several nuclear proteins as STI1 interactors. Overexpression of one of these interactors, PIAS1, seems to be specifically involved in STI1 nuclear retention and in directing STI1 and Hsp90 to specific sub-nuclear regions. PIAS1 and STI1 co-immunoprecipitate and PIAS1 can function as …
The Prion Protein Ligand, Stress-Inducible Phosphoprotein 1, Regulates Amyloid-Beta Oligomer Toxicity, Valeriy G. Ostapchenko, Flavio H. Beraldo, Amro H. Mohammad, Yu-Feng Xie, Pedro H. F. Hirata, Ana C. Magalhaes, Guillaume Lamour, Hongbin Li, Andrzej Maciejewski, Jillian C. Belrose, Bianca L. Teixeira, Margaret Fahnestock, Sergio T. Ferreira, Neil R. Cashman, Glaucia N. M. Hajj, Michael F. Jackson, Wing-Yiu Choy, John F. Macdonald, Vilma R. Martins, Vania F. Prado, Marco A. M. Prado
The Prion Protein Ligand, Stress-Inducible Phosphoprotein 1, Regulates Amyloid-Beta Oligomer Toxicity, Valeriy G. Ostapchenko, Flavio H. Beraldo, Amro H. Mohammad, Yu-Feng Xie, Pedro H. F. Hirata, Ana C. Magalhaes, Guillaume Lamour, Hongbin Li, Andrzej Maciejewski, Jillian C. Belrose, Bianca L. Teixeira, Margaret Fahnestock, Sergio T. Ferreira, Neil R. Cashman, Glaucia N. M. Hajj, Michael F. Jackson, Wing-Yiu Choy, John F. Macdonald, Vilma R. Martins, Vania F. Prado, Marco A. M. Prado
Anatomy and Cell Biology Publications
In Alzheimer's disease (AD), soluble amyloid-beta oligomers (A beta Os) trigger neurotoxic signaling, at least partially, via the cellular prion protein (PrPC). However, it is unknown whether other ligands of PrPC can regulate this potentially toxic interaction. Stress-inducible phosphoprotein 1 (STI1), an Hsp90 cochaperone secreted by astrocytes, binds to PrPC in the vicinity of the A beta O binding site to protect neurons against toxic stimuli. Here, we investigated a potential role of STI1 in A beta O toxicity. We confirmed the specific binding of A beta Os and STI1 to the PrP and showed that STI1 efficiently inhibited A …
Role Of Alpha 7 Nicotinic Acetylcholine Receptor In Calcium Signaling Induced By Prion Protein Interaction With Stress-Inducible Protein 1, Flavio H. Beraldo, Camila P. Arantes, Tiago G. Santos, Nicolle G. T. Queiroz, Kirk Young, Jane R. Rylett, Regina P. Markus, Marco A. M. Prado, Vilma R. Martins
Role Of Alpha 7 Nicotinic Acetylcholine Receptor In Calcium Signaling Induced By Prion Protein Interaction With Stress-Inducible Protein 1, Flavio H. Beraldo, Camila P. Arantes, Tiago G. Santos, Nicolle G. T. Queiroz, Kirk Young, Jane R. Rylett, Regina P. Markus, Marco A. M. Prado, Vilma R. Martins
Anatomy and Cell Biology Publications
The prion protein (PrP(C)) is a conserved glycosylphosphatidyl-inositol-anchored cell surface protein expressed by neurons and other cells. Stress-inducible protein 1 (STI1) binds PrP(C) extracellularly, and this activated signaling complex promotes neuronal differentiation and neuroprotection via the extracellular signal-regulated kinase 1 and 2 (ERK1/2) and cAMP-dependent protein kinase 1 (PKA) pathways. However, the mechanism by which the PrPC-STI1 interaction transduces extracellular signals to the intracellular environment is unknown. We found that in hippocampal neurons, STI1-PrP(C) engagement induces an increase in intracellular Ca(2+) levels. This effect was not detected in PrP(C)-null neurons or wild-type neurons treated with an STI1 mutant unable to …