ArticleJournal of molecular neuroscience : MN2011
A novel PrP partner HS-1 associated protein X-1 (HAX-1) protected the cultured cells against the challenge of H₂O₂.
Article in Journal of molecular neuroscience : MN, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Extensive Disturbances of Intracellular Components and Dysfunctions of Biological Pathways in the Brain Tissues During Prion Infection - China's Studies.China CDC weekly · 2022Review
- The type III secretion system effector EspO of enterohaemorrhagic Escherichia coli inhibits apoptosis through an interaction with HAX-1.Cellular microbiology · 2021Article
- Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction.International journal of molecular sciences · 2020Review
- Intrinsically disordered HAX-1 regulates CaBiochimica et biophysica acta. Biomembranes · 2020Article
- Abnormally upregulated αB-crystallin was highly coincidental with the astrogliosis in the brains of scrapie-infected hamsters and human patients with prion diseases.Journal of molecular neuroscience : MN · 2013Article
- PrP octarepeats region determined the interaction with caveolin-1 and phosphorylation of caveolin-1 and Fyn.Medical microbiology and immunology · 2013Article
- Activation of the macroautophagic system in scrapie-infected experimental animals and human genetic prion diseases.Autophagy · 2012Article
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Authors and funding
13 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prion protein (PrP) is a ubiquitous conserved glycoprotein predominantly expressed in neurons of the central nervous system (CNS). To elucidate on its cellular function, we performed a yeast two-hybrid screen within an adult human brain cDNA library for potential PrP-binding molecules. A novel protein, HS-1 associated protein X-1 (HAX-1), was identified to be able to bind with PrP strongly. The interaction between the two proteins has been further verified by glutathione-S-transferase (GST) pull-down and immunoprecipitation assays. The minimal binding regions were mapped to the segments of residues aa 91-163 for PrP(C) and residues aa 38-129 for HAX-1. Immunofluorescent assays of co-expressions of human PrP and HAX-1 in 293T and SHSY-5Y cells revealed marked co-localizations of those two proteins in cytoplasm. Moreover, the co-expression of HAX-1 and wild-type PrP (PG5) was found to enhance the cellular resistance to the challenge of H₂O₂. Contrarily, co-transfection of HAX-1 did not reverse but aggravated the cytotoxicities of the genetic CJD (gCJD) associated PrP mutants with nine- (PG9) and fourteen-octarepeats (PG14). Our data provide for the first time a new PrP-interacting partner that may play role in cell oxidative stress and anti-apoptosis physiologically and cell damage pathologically.
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