title: Detecting HSP90 phosphorylation.
abstract: Heat-shock protein 90 (HSP90) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis. HSP90's ATPase activity is associated with its chaperone function. Co-chaperones as well as posttranslational modifications (phosphorylation, acetylation, and S-nitrosylation) are important for regulating its ATPase activity. Yeast can be used to express and purify HSP90 and also detect its phosphorylation by pan-phosphoserine or phosphothreonine antibodies.
authors: Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
authors: Mehdi
authors: M
authors: Mollapour
authors: Len
authors: L
authors: Neckers
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D018841:HSP90 Heat-Shock Proteins; D000251:Adenosine Triphosphatases