NDLI: Regulation of stress-inducible phosphoprotein 1 nuclear retention by protein inhibitor of activated STAT PIAS1.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Soares, Iaci N. Caetano, Fabiana A. Pinder, Jordan Rodrigues, Bruna Roz Beraldo, Flavio H. Ostapchenko, Valeriy G. Durette, Chantal Pereira, Grace Schenatto Lopes, Marilene H. Queiroz-Hazarbassanov, Nicolle Cunha, Isabela W. Sanematsu, Paulo I. Suzuki, Sergio Bleggi-Torres, Luiz F. Schild-Poulter, Caroline Thibault, Pierre Dellaire, Graham Martins, Vilma R. Prado, Vania F. Prado, Marco A. M.
Description	Author Affiliation: Soares IN ( Robarts Research Institute, The University of Western Ontario, London, ON, Canada)
Abstract	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 an E3 SUMO ligase for STI. Using mass spectrometry we identified five SUMOylation sites in STI1. A STI1 mutant lacking these five sites is not SUMOylated, but still accumulates in the nucleus in response to increased expression of PIAS1, suggesting the possibility that a direct interaction with PIAS1 could be responsible for STI1 nuclear retention. To test this possibility, we mapped the interaction sites between PIAS1 and STI1 using yeast-two hybrid assays and surface plasmon resonance and found that a large domain in the N-terminal region of STI1 interacts with high affinity with amino acids 450-480 of PIAS1. Knockdown of PIAS1 in astrocytes impairs the accumulation of nuclear STI1 in response to irradiation. Moreover, a PIAS1 mutant lacking the STI1 binding site is unable to increase STI1 nuclear retention. Interestingly, in human glioblastoma multiforme PIAS1 expression is increased and we found a significant correlation between increased PIAS1 expression and STI1 nuclear localization. These experiments provide evidence that direct interaction between STI1 and PIAS1 is involved in the accumulation of nuclear STI1. This retention mechanism could facilitate nuclear chaperone activity.
File Format	HTM / HTML
ISSN	15359476
e-ISSN	15359484
DOI	10.1074/mcp.M113.031005
Journal	Molecular & Cellular Proteomics
Issue Number	11
Volume Number	12
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2013-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Proteomics Astrocytes Metabolism Heat-shock Proteins Protein Inhibitors Of Activated Stat Animals Cytology Radiation Effects Cell Death Genetics Physiology Cell Nucleus Cells, Cultured Dna Damage Gamma Rays Gene Knockdown Techniques Hek293 Cells Haploinsufficiency Deficiency Mice Mice, Inbred C57bl Mice, Knockout Antagonists & Inhibitors Protein Interaction Maps Recombinant Fusion Proteins Stress, Physiological Sumoylation Two-hybrid System Techniques Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Medicine Analytical Chemistry Molecular Biology Biochemistry

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Regulation of Stress-Inducible Phosphoprotein 1 Nuclear Retention by Protein Inhibitor of Activated STAT PIAS1

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